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PubMed2002

P311 induces a TGF-beta1-independent, nonfibrogenic myofibroblast phenotype.

P311, also called PTZ17, was identified by suppressive subtraction hybridization as potentially involved in smooth muscle (SM) myogenesis. P311 is an 8-kDa protein with several PEST-like motifs found in neurons and muscle. P311 transfection into two fibroblast cell lines, NIH 3T3 and C3H10 T1/2, induced phenotypic changes consistent with myofibroblast transformation, including upregulation of SM alpha-actin and SM22, induction of FGF-2, VEGF, PDGF, and PDGF receptors, upregulation of integrins alpha3 and alpha5, and increased proliferation rate. The P311-mediated changes differed, however, from the well-characterized myofibroblast in that P311 inhibited TGF-beta1, TGF-beta receptor 2, and TGF-beta1-activating MMP-2 and MMP-9, with the resultant decrease in collagen 1 and 3 expression. The effect of P311 on collagen was overcome by exogenous TGF-beta1, indicating that the cells were responsive to TGF-beta1 paracrine stimulus. In support of a role for P311 in vivo, immunohistochemical examination of human wounds showed P311 only in myofibroblasts and their activated precursors. To our knowledge, these studies are the first to implicate P311 in myofibroblast transformation, to demonstrate that transformation may occur independently of TGF-beta1, and to suggest that P311 may prevent fibrosis.

3T3 Cells↗

PubMed1995

Changes in integrin expression during chondrogenesis in vitro: an immunomorphological study.

Integrins are receptors composed of ligand-specific alpha-chains and cell type-specific beta-chains which are involved in cell-cell and cell-matrix interactions. The distribution of alpha 1- and alpha 3-integrins as well as collagen Types I and II, was investigated by immunofluorescence and immunoelectron microscopy during chondrogenesis in organ culture after various culture periods. Mesenchymal cells from limb buds of Day 12 mouse embryos were grown at high density. Within the first 2 days of the culture period, only alpha 1-integrin could be detected. Formation of cartilage-specific matrix on Day 3 was accompanied by the occurrence of alpha 3-integrin. On Day 7, alpha 3 was present only in cartilage nodules, whereas alpha 1 was strongly expressed in the perichondrium and was more or less homogeneously distributed in the surrounding mesenchyme. On Day 14, alpha 1-integrin was again detectable in cartilage. We suggest that the change in collagen formation from Type I to Type II during chondrogenesis is accompanied by a change in integrin expression from alpha 1 to alpha 3. Conversely, dedifferentiation of chondrocytes in aging cartilage is accompanied by the occurrence of collagen Type I and alpha 1-integrin. Therefore, a strict correlation between the collagen type synthesized by the cells and the appropriate receptor presented by the cells is suggested.

Animals↗

PubMed2003

Differential regulation of cell adhesive functions by integrin alpha subunit cytoplasmic tails in vivo.

Cell adhesion to fibronectin (FN) is crucial for early vertebrate morphogenesis. In Xenopus gastrulae, several distinct integrin-dependent adhesive behaviors can be identified: adhesion of cells to FN, assembly of FN fibrils, and initiation of cell spreading and migration in response to mesoderm inducing signals. We have taken a chimeric integrin approach to investigate the role of the integrin alpha cytoplasmic tail in the specification of these developmentally significant adhesive functions. Cytoplasmic tail-deleted alpha4 constructs and alpha4-ectodomain/alpha-cytoplasmic tail chimeras were generated and expressed in whole embryos. Normal gastrula cells lack integrin alpha4 and, correspondingly, are unable to adhere to the alpha4 ligand, the V-region of FN. The ability of alpha4 constructs to promote adhesive behaviors was established by placing tissue explants or dissociated cells on an FN V-region fusion protein that lacks the RGD (Arg-Gly-Asp)/synergy sites or treating whole embryos with antibodies that block endogenous integrin-FN interactions. We found that each alpha4 cytoplasmic domain deletion mutant and alpha-tail chimera examined could support cell attachment; however, activin induction-dependent cell spreading, mesoderm cell and explant motility, and the ability to assemble FN matrix on the blastocoel roof varied with specific alpha subunit tail sequences. These data suggest that alpha cytoplasmic tail signaling and changes in integrin activation state can regulate a variety of developmentally significant adhesive behaviors in both space and time.

Activins↗

PubMed1995

Alpha v and alpha 3 integrin subunits are associated with myofibrils during myofibrillogenesis.

The development of the myofibrillar apparatus in skeletal muscle is a process in which transmembrane linkages with adhesion molecules are implicated. Integrins are one class of transmembrane adhesion receptors which appear to mediate these interactions. Two prominent linkages are at the myotendinous junction (MTJ), which residues at the ends of the cell and connects myofibrils to the tendon, and the costameres, which encircle the girth of the cell and connect the Z-disks to the sarcolemma. In this study we report that the alpha v integrin subunit is a prominent component of the costamere. The alpha v subunit is present initially on developing myotubes in a diffuse staining pattern with some concentration along nascent myofibrils. However, it appears in a striated pattern at the costamere and inconsistently at the M-line following the striation of alpha-actinin and titin but before that of desmin. Its recruitment to preformed striation suggests that it is incorporated into a pre-existing structure. The presence of alpha v in the costamere points to a role in lateral myofibrillar anchorage. In addition, we find that the alpha 3 subunit is transiently associated with myofibrils along portions of their lengths and at their ends during myofibrillogenesis. The alpha 3 subunit staining shows a novel localization and junctional structure. As myofibrils become striated the alpha 3 integrin dissociates from the localized pattern and becomes diffuse. This suggests a possible role in the stabilization of nascent myofibrils prior to striation. Antibody-induced perturbation of adhesion mediated by the integrin beta 1 subunit in developing myotubes inhibits assembly of the sarcomeric architecture.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗

PubMed1995

Alpha v and alpha 3 integrin subunits are associated with myofibrils during myofibrillogenesis.

The development of the myofibrillar apparatus in skeletal muscle is a process in which transmembrane linkages with adhesion molecules are implicated. Integrins are one class of transmembrane adhesion receptors which appear to mediate these interactions. Two prominent linkages are at the myotendinous junction (MTJ), which resides at the ends of the cell and connects myofibrils to the tendon, and the costameres, which encircle the girth of the cell and connect the Z-disks to the sarcolemma. In this study we report that the alpha v integrin subunit is a prominent component of the costamere. The alpha v subunit is present initially on developing myotubes in a diffuse staining pattern with some concentration along nascent myofibrils. However, it appears in a striated pattern at the costamere and inconsistently at the M-line following the striation of alpha-actinin and titin but before that of desmin. Its recruitment to preformed striation suggests that it is incorporated into a pre-existing structure. The presence of alpha v in the costamere points to a role in lateral myofibrillar anchorage. In addition, we find that the alpha 3 subunit is transiently associated with myofibrils along portions of their lengths and at their ends during myofibrillogenesis. The alpha 3 subunit staining shows a novel localization and junctional structure. As myofibrils become striated the alpha 3 integrin dissociates from the localized pattern and becomes diffuse. This suggests a possible role in the stabilization of nascent myofibrils prior to striation. Antibody-induced perturbation of adhesion mediated by the integrin beta 1 subunit in developing myotubes inhibits assembly of the sarcomeric architecture.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗

PubMed1999

(Alpha)3(beta)1 integrin regulates epithelial cytoskeletal organization.

Epithelial cell morphology and cytoskeletal organization are determined by interactions, with both adjacent cells and the extracellular matrix, which are mediated by integrins and cadherins. Little is known, however, of the relative contributions of integrins and cadherins to maintaining the sub-cortical cytoskeleton characteristic of epithelial cells. Since most studies that utilize integrin-blocking antibodies result in a loss of both cell-cell adhesion and sub-cortical cytoskeletal organization, it has been difficult to distinguish whether integrins and cadherins both mediate cytoskeletal assembly in epithelial cells. Therefore, cells derived from kidney collecting ducts of (alpha)3(beta)1 integrin-deficient mice were used to examine the role of integrins in epithelial cell morphology and cytoskeletal organization. In primary cell culture, (alpha)3(beta)1 integrin-deficient kidney collecting duct cells maintain cadherin-mediated cell-cell adhesions but fail to form the sub-cortical cytoskeleton that is characteristic of epithelial cells, and instead assemble actin stress fibers. Moreover, the cell-cell junctions in mutant cells were irregular, rather than being uniformly oriented perpendicular to the culture substrate. These results demonstrated that integrins have an primary and essential function in establishing and maintaining the sub-cortical cytoskeleton that is characteristic of epithelial cells. To further study the role of (alpha)3(beta)1 integrin in establishing and maintaining cytoskeletal organization in tubular epithelial cells, we derived immortalized cell lines from wild-type and (alpha)3(beta)1 integrin-deficient kidney collecting ducts that duplicated the cytoskeletal and cadherin organization observed in primary cells. E-cadherin and (alpha)- and (beta)-catenin were complexed together in equal amounts in membranes of wild-type and (alpha)3(beta)1 integrin-deficient cells. However, association of the cadherin:catenin complex with (alpha)-actinin was greatly decreased in mutant cells, indicating that integrin-mediated assembly of the sub-cortical cytoskeleton is essential for subsequent association of the cytoskeleton with the cadherin:catenin complex. These results present direct evidence for integrin:cadherin cross-regulation in which cadherin function is dependent on the presence of an integrin.

Animals↗

PubMed2000

Lymphoid adhesion promotes human thymic epithelial cell survival via NF-(kappa)B activation.

Inside the thymus, thymic epithelial cells and thymocytes show an interdependent relationship for their functional differentiation and development. As regards possible interdependency for their mutual survival, it is clear that lympho-epithelial adhesion can control the survival of developing thymocytes whereas the effects of lymphoid adhesion on epithelial cell survival have never been described. To address this issue, we performed co-cultures between normal human thymic epithelial cells (TEC) and a mature lymphoid T cell line (H9) or unfractionated thymocytes. TEC were induced to apoptosis by growth factor deprivation and the level of cell death was measured by flow cytometry. TEC stimulated by cell adhesion showed a significant reduced apoptosis when compared to the control and this phenomenon was associated with increased binding activity of NF-(kappa)B, as measured by gel shift analysis. The activation of NF-(kappa)B was necessary to promote survival, since its inhibition by acetyl salicylic acid prevented the promoting effect. The mAb-mediated crosslinking of (alpha)(3)(beta)(1) was considered as a potential inducer of TEC survival, since we have previously demonstrated that the engagement of this integrin was able to induce NF-(kappa)B activation in TEC. The crosslinking of (alpha)(3)(beta)(1), which clustered at the lympho-epithelial contact sites, partially reproduced the promoting activity of cell adhesion. These results highlight that lympho-epithelial adhesion can control the survival of thymic epithelial cells through an intracellular pathway which requires the activation of NF-(kappa)B and is triggered by integrins of the (beta)(1) family.

Antigens, CD↗

PubMed2000

Interaction between the cytodomains of the alpha 3 and beta 1 integrin subunits regulates remodelling of adhesion complexes on laminin.

The first step of laminin 1-induced signal transduction is initiated by the formation of alpha 6 beta 1 integrin-specific adhesion complexes. In contrast, on other laminin isoforms the adhesion complexes are alpha 3 beta 1 integrin-specific due to a transdominant regulation of the alpha 6 beta 1 integrin by the alpha 3 beta 1 integrin. To determine the mechanism of this regulation, peptides representing the cytoplasmic domain of the alpha 3 or alpha 6 integrin subunits were microinjected together with recombinant enhanced green fluorescence protein into live fibroblasts. Microinjection of the alpha 3 integrin peptide to laminin 1-adherent cells displaying alpha 6 beta 1 integrin-specific adhesion complexes resulted in the disengagement of the alpha 6 beta 1 integrin, while microinjection of green fluorescence protein alone or in combination with the alpha 6 integrin cytodomain had no effect. Further surface plasmon resonance studies revealed that the cytodomain of the beta 1 integrin subunit interacts with low affinity with the cytoplasmic tail of the alpha 3 integrin subunit, but not with that of several other alpha subunits including alpha 6. These results imply that the cytoplasmic tails of the integrin alpha subunits play a critical role in the regulation of integrin-induced signal transduction. In particular, the intracellular tail of the alpha 3 integrin subunit controls the formation of adhesion complexes in cells adhering to laminins.

Amino Acid Sequence↗

PubMed1996

Reduction of tumorigenicity by alpha 3 integrin in a rhabdomyosarcoma cell line.

The expression levels of integrin adhesion receptors have often been correlated with neoplastic transformation and invasiveness. To investigate more definitively the role of the integrin VLA-3 (alpha 3 beta 1) in tumor cell behavior, we transfected alpha 3 subunit cDNA into human rhabdomyosarcoma (RD) cells. Transfectants expressing high levels of alpha 3 beta 1 on their cell surface displayed an altered morphology and decreased anchorage-dependent growth in vitro. Cells expressing alpha 3 also displayed marked reduction in anchorage-independent growth in soft agar and in their ability to form tumors when injected subcutaneously into athymic nude mice. Thus, VLA-3 can repress the transformed phenotype of rhabdomyosarcoma tumor cells. Similar changes in morphology and growth characteristics were observed in cells expressing a chimeric molecule X3C4 in which the alpha 3 cytoplasmic domain had been exchanged with that of the alpha 4 integrin subunit. Therefore, alpha 3 inhibitory effects in RD cells appear not to require specific signalling through the alpha 3 cytoplasmic domain.

Amino Acid Sequence↗

PubMed1999

Isolation of protein kinase C-alpha-regulated cDNAs associated with breast tumor aggressiveness by differential mRNA display.

Elevated levels of protein kinase C (PKC) are associated with increased metastatic capacity in both human breast cancer cells and breast tumors. MCF-7 breast cancer cells stably transfected with PKC-alpha were recently shown to display a more aggressive phenotype and increased tumorigenicity in nude mice. To identify genes involved in the progression to the aggressive phenotype, mRNA differential display was performed to isolate cDNAs that are differentially expressed between the parental, non-metastatic MCF-7 cell line and the metastatic derivative MCF-7-PKC-alpha cell line. One cDNA was identified which was upregulated and four cDNAs were downregulated in MCF-7-PKC-alpha cells. The upregulated cDNA may be a differentiation-specific gene as it is 100% homologous to a putative glialblastoma cell differentiation-related protein, GBDR1. DNA sequence analysis and flow cytometry revealed that three of the downregulated cDNAs correspond to histone 3.B, and integrins alpha3 and alpha6. The fourth downregulated cDNA clone, G2Q, is a novel sequence. G2Q is expressed in normal breast and bronchial tissue, but is downregulated in a variety of tumor cell lines and in aggressive primary and secondary breast tumors, suggesting that G2Q may be a useful prognostic indicator of tumor aggressiveness. Further, downregulation of G2Q expression in the non-metastatic MCF-7 cells by antisense oligonucleotides resulted in increased in vitro invasive capacity of these cells in a Matrigel matrice. This study provides the basis for identifying new genes involved in breast tumor progression and the role that PKC plays in the pathogenesis of this cancer.

Base Sequence↗

PubMed2001

The novel monoclonal antibody MH8-4 inhibiting cell motility recognizes integrin alpha 3: inverse of its expression withmetastases in colon cancer.

The molecular basis of cell motility is obviously highly complex and is considered to be controlled by a number of molecular systems including cell adhesion molecules, their receptors, cytoskeletal components, a junctional unit connecting cytoskeletal components and membrane receptors, and various peptide growth factors. The possible involvement of proteins at the cell surface in controlling cell motility has been systematically investigated. Previously, we have addressed this question using functional monoclonal antibodies (MAbs), which inhibit cell motility as probes. In order to further identify cell surface molecules involved in metastasis of gastrointestinal tumors, the present study utilized an approach based on the selection of a colon cancer cell line RPMI4788, which showed high motility out of a large number of human gastrointestinal tumor cell lines. MAb MH8-4 was established after immunization of mice with RPMI4788 and selected on the basis of inhibition of RPMI4788 cell migration in a transwell penetration assay. MH8-4 inhibited the phagokinetic tract motility of various cancer cell lines. A cDNA cloning revealed that MH8-4 recognized a specific protein structure, integrin alpha 3. In order to determine whether these experimental results are of relevance with respect to actual human gastrointestinal tumors, we investigated integrin alpha 3 expression in 40 colon cancers with distant metastases. Our immunohistochemical study showed that in almost 27.5% of the cases, the metastatic tumors had lower integrin alpha 3 levels than their corresponding primary tumors. Moreover, there were no primary tumors with lower integrin alpha 3 expression than their corresponding metastatic tumors. Our data suggest that low integrin alpha 3 expression may be associated with the metastatic potential of certain colon cancers.

Antibodies, Monoclonal↗

PubMed2005

Role of extracellular matrix in regulation of staurosporine-induced apoptosis in breast cancer cells.

Autocrine and paracrine mechanisms modulate the synthesis and secretion of extracellular matrix (ECM); moreover, each component of the ECM is capable of modulating the synthesis and release of other ECM molecules. Therefore, the synthesis of ECM glycoprotein fibronectin and laminin was studied in the human breast cancer cell lines MCF7 and MDA MB 23, plated on different ECM. Our results showed that the cells plated on a fibronectin substrate increased laminin synthesis: this event correlated with an increase in alpha2 and alpha3 integrin subunits. Staurosporine-induced apoptosis was then analyzed in the cell lines plated on different ECM. Staurosporine treatment determined the apoptosis of 35 and 33% respectively of MDA MB 231 and MCF7; these values increased to 60 and 64% in cells plated on laminin, to 48 and 63% in cells plated on fibronectin and to 64 and 69% in cells plated on matrigel. Moreover, staurosporine treatment decreased bcl-2 expression in the cells plated on fibronectin and laminin. Yet, staurosporine treatment determined PARP cleavage and PARP partial disappearance when the cells were plated on matrigel. Finally, a partial loss of function mutant Ras protein that activated only Raf pathway, was expressed in MCF7, in order to identify whether the increase of apoptosis induced by extracellular matrix involved the Raf/MAP kinase pathway. The increase of apoptosis of the cells plated on matrigel suggested that the activation of the Raf pathway is probably involved in the decrease of survival on matrigel. These data demonstrate that the modification of ECM modulates the apoptotic process of breast cancer cells and suggest that it is worthwhile to dissect the role of ECM in the control of apoptotic process.

Apoptosis↗

PubMed2000

Potent costimulation of effector T lymphocytes by human collagen type I.

Purified, resting peripheral blood T lymphocytes were previously reported to undergo beta(1) integrin-dependent activation when cultured with anti-CD3 mAb coimmobilized with fibronectin, but not type I collagen. However, the extravascular T cells that encounter immobilized extracellular matrix proteins and are involved in disease pathogenesis have different properties from resting peripheral blood cells. In this study, we confirm that resting CD4(+) and CD8(+) T cells from peripheral blood are costimulated by immobilized fibronectin, but not type I collagen. In contrast, Ag- or mitogen-stimulated CD4(+) and CD8(+) T cell lines, used as models of the effector cells involved in disease, are more potently costimulated by type I collagen than fibronectin. The collagen-induced effects are similar in assays with serum-free medium and in more physiological assays in which anti-CD3 mAb is replaced by a threshold concentration of Ag and irradiated autologous PBMC as APC. The responses are beta(1) integrin dependent and mediated largely by very late Ag (VLA) 1 and 2, as shown by their up-regulation on the T cell lines as compared with freshly purified resting PBL, and by the effects of blocking mAb. Reversed phase HPLC located the major costimulatory sequence(s) in the alpha1 chain of type I collagen, the structure of which was confirmed by amino acid sequencing. The results demonstrate the potential importance of type I collagen, an abundant extracellular matrix protein, in enhancing the activation of extravascular effector T cells in inflammatory disease, and point to a new immunotherapeutic target.

Adjuvants, Immunologic↗

PubMed1998

Correlation of lining thickness and expression of alpha 2 and alpha 3 integrins within the epithelial lining of odontogenic cysts.

Using monoclonal antibodies, we performed immunohistochemical investigations of the expression of alpha 2, alpha 3 and beta 4 integrin subunits within the squamous epithelial linings of odontogenic cysts. Tissue samples consisted of both follicular cysts and odontogenic keratocysts from 15 patients. It was found that beta 4 integrin was expressed on the basement membrane regardless of the histological type of the cyst. The degree of immunostaining for alpha 2 and alpha 3 integrin expression corresponded to the thickness of the epithelial cyst wall. We found that the thickness of the epithelial lining of odontogenic cysts had a direct correlation with the expression of integrin molecules.

Antigens, CD↗

PubMed2000

[The possible role of adhesion molecule, alpha 3 integrin, in the synthesis of intracrescentic extracellular matrix in accelerated anti-GBM nephritis].

Studies were performed on the behavior of crescent-composing cells of crescent glomerulonephritis induced by the injection of anti-GBM antibody to WKY rats. alpha 3 integrin, podocalyxin and ED1 were stained immunohistochemically as markers of parietal, visceral epithelial cells, and macrophages, respectively. Cellular fibronectin (cFn) and type I collagen were also stained in the same manner. Fluoresceine- and Rhodamine-conjugated IgGs were used as second antibodies for double staining to show the geographic relation of the two target molecules. Morphological examinations were performed at day 7, 14 and 28 after disease induction. Periodic acid-methenamine-silver (PAM) and Azan staining showed time-dependent increase in extension and cellularity. PAM-positive intracrescentic fibers were likewise increased, which was related to an increased frequency of ruptured capsules. Intracrescentic cFn increasing in parallel with PAM-positive fibers and type I collagen, was remarkably stained at day 28. Intracrescentic ED1-positive cells showed also a significant increase at day 28. Podocalyxin was not stained in the crescent, while ED1 and alpha 3 integrin were remarkably stained. Double staining showed apposition of cFn and alpha 3 integrin, indicating close contact of these molecules, but such apposition was not observed between ED1 and cFn. These findings indicate that ED1 and alpha 3 integrin--(possibly visceral cell derived) positive cells occupy significant cellular components of the crescent and that the latter plays a part in synthesis of the intracrescentic extracellular matrix.

Animals↗

PubMedDate not supplied

Culture conditions modulate cell phenotype and cause selection of subpopulations in PC3 prostate cancer cell line.

PC3 cell line contains different cell variants. A first variant grows as spherical multicellular aggregates and shows anchorage-independent growth. A second variant grows as single small rounds and shows anchorage-dependent growth without cell spreading. A third variant, representing the most abundant population, grows as adherent cells. These populations differ in alpha 2 beta 1 and alpha 3 beta 1 integrin expression with low levels in the suspended (S) cells, intermediate in partially adherent (R) cells and high in adherent cells (A). TPA, which up-regulates the expression of beta 1 integrins, increases invasiveness of cells. In addition, PC3 variants differ in MMP9 and uPA secretion and activity. High levels of TIMP1 and PAI1 present in S variant reduce MMP9 and uPA activities, respectively. In conclusion, PC3 cell line shows variants with strong phenotypic heterogeneity reflecting also the in vitro culture condition. Our observations may explain some of the contradictions in the literature. Therefore, the data obtained with this line should be evaluated more carefully, considering morphological and functional characteristics of the possible variants in the cell population. However, this heterogeneity may represent a good model in the study of tumor progression.

Antigens, CD↗

PubMed2000

[Expression of alpha 1-4 integrins in hypertrophic scar fibroblasts].

OBJECTIVE: To determine the expression levels of alpha 1-4 integrins in hypertrophic scar fibroblasts and investigate the role that alpha 1-4 integrins may play in the process of hypertrophic scar formation. METHODS: The membrane protein was extracted from hypertrophic scar and normal skin tissues. The content of alpha 1-4 integrins of the membrane protein was detected by immunoblotting method. The locations of alpha 1-4 integrin expression were examined by immunohistochemical stain. RESULTS: 1. Higher concentration of alpha 1-4 integrins was identified in the membrane protein extracted from hypertrophic scar than from normal skin. 2. In normal skin, the expression of alpha 1, alpha 2 and alpha 3 integrins located on the epidermal cell surface but not on the dermal fibroblast surface. In the hypertrophic scar, not only did the epidermal cell surface express alpha 1-3 integrins, but also the fibroblast surface expressed alpha 1-4 integrins. CONCLUSIONS: The expressions of hypertrophic scar fibroblast surface integrins are subjected not only to cell-extracellular matrix adhesion, but also to intracellular/extracellular signal transduction. Integrins may play an important role in regulating much of fibroblast behavior, including growth, differentiation, phenotype, and in scar tissue remodelling.

Adolescent↗

PubMed1999

[Study on the effect of ligustrazine on adherent molecule expression of bone marrow cells in immune-mediated aplastic anemia mice].

OBJECTIVE: To explore the effect of ligustrazine on the expression of adherent molecule of bone marrow cells in immune-mediated aplastic anemia(AA) mice. METHODS: Each immune-mediated AA mouse was intraperitoneally injected with 5 mg ligustrazine twice a day. On the 14th day, expressions of CD49d and CD49c in bone marrow mononuclear cells(MNC) were detected by flow cytometry, and VCAM-1 on stromal cells by immunohistochemistry SABC. RESULTS: Expressions of CD49d, CD49e and VCAM-1 were significantly lower in AA group than in normal group(t = 11.96, 17.18 and 7.09 respectively, P < 0.001), and were much higher in ligustrazine treated group than in non-treated group(t = 9.05, 14.61 and 6.91 respctively, P < 0.001). Expressions of CD49d and VCAM-1 were in the normal range in ligustrazine group. CONCLUSIONS: Ligustrazine can increase the expression of adherent molecule of bone marrow cells in immune-mediated AA mice, thus promote the growth of hematopoietic cells.

Anemia, Aplastic↗