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Biomedical subjects

M D Basson

Publications and source records attributed to M D Basson.

At least 19 recordsLinked to original sources
PubMed2006

Extracellular pressure stimulates tumor cell adhesion in vitro by paxillin activation.

Metastasizing colon cancer cells bind target tissues primarily via integrins. Extracellular pressure or shear stress stimulates integrin-mediated adhesion to matrix proteins or endothelial cells by activating the focal adhesion proteins FAK and Src. Because this effect is blocked by cytoskeletal perturbation and paxillin may link the cytoskeleton to the focal adhesion complex, we evaluated the role of paxillin in pressure-induced malignant colonocyte adhesion. We studied SW620 colon cancer cells and confirmed key results in Caco-2 colon cancer cells, primary human colon cancer cells, and a murine colonic adenocarcinoma. We evaluated adhesion to collagen at ambient and 15 mmHg increased pressure after 30 minutes, and paxillin, FAK, and Src phosphorylation in suspended cells prior to adhesion. Some cells were treated with siRNA to paxillin or FAK, or the Src inhibitor PP2. We also compared pressure-induced signals in suspended cells with adhesion-induced signals after adhesion to collagen. Pressure stimulated adhesion and paxillin phosphorylation in SW620 and Caco-2 cells and human primary colon cancer cells. Pressure also increased paxillin phosphorylation in murine carcinoma cells. SiRNA to paxillin decreased SW620 and Caco-2 paxillin without altering basal levels of phosphorylated paxillin. Paxillin reduction decreased basal adhesion to collagen, and inhibited pressure-stimulated adhesion, as well as paxillin, FAK397, FAK576, and Src476 phosphorylation. Neither PP2 nor siRNA to FAK inhibited induction of paxillin phosphorylation by pressure. In contrast, adhesion stimulated FAK, Src, and paxillin phosphorylation regardless of paxillin reduction. In summary, pressure induced paxillin phosphorylation in colon cancer cells. Paxillin reduction inhibited basal adhesion and blocked the pressure-mediated increase in adhesion, as well as pressure-induced FAK and Src signals, while adhesion-induced signals were preserved. Paxillin may be an upstream mediator of pressure-stimulated adhesion, important in metastasis.

Adenocarcinoma↗
PubMed2004

Extracellular pressure stimulates colon cancer cell proliferation via a mechanism requiring PKC and tyrosine kinase signals.

UNLABELLED: Pressure in colonic tumours may increase during constipation, obstruction or peri-operatively. Pressure enhances colonocyte adhesion by a c-Src- and actin-cytoskeleton-dependent PKC-independent pathway. We hypothesized that pressure activates mitogenic signals. METHODS: Malignant colonocytes on a collagen I matrix were subjected to 15 mmHg pressure. ERK, p38, c-Src and Akt phosphorylation and PKCalpha redistribution were assessed by western blot after 30 min and PKC activation by ELISA. Cells were counted after 24 h and after inhibition of each signal, tyrosine phosphorylation or actin depolymerization. RESULTS: Pressure time-dependently increased SW620 and HCT-116 cell counts on collagen or fibronectin (P < 0.01). Pressure increased the SW620 S-phase fraction from 28 +/- 1 to 47 +/- 1% (P = 0.0002). Pressure activated p38, ERK, and c-Src (P < 0.05 each) but not Akt/PKB. Pressure decreased cytosolic PKC activity, and translocated PKCalpha to a membrane fraction. Blockade of p38, ERK, c-Src or PI-3-K or actin depolymerization did not inhibit pressure-stimulated proliferation. However, global tyrosine kinase blockade (genistein) and PKC blockade (calphostin C) negated pressure-induced proliferation. CONCLUSIONS: Extracellular pressure stimulates cell proliferation and activates several signals. However, the mitogenic effect of pressure requires only tyrosine kinase and PKCalpha activation. Pressure may modulate colon cancer growth and implantation by two distinct pathways, one stimulating proliferation and the other promoting adhesion.

CSK Tyrosine-Protein Kinase↗
PubMed2001

In vitro evidence for matrix regulation of intestinal epithelial biology during mucosal healing.

We now know that restitution is more than a process of dedifferentiation and random cell movement across a wound defect. In fact, it is an orderly and regulated process in which gut mucosal epithelial cells adopt a migratory phenotype involving alterations in the cytoskeleton and intracellular motors likely to be tightly regulated by integrin-associated signal proteins and downstream second messengers. The extracellular matrix influences restitution not only as a physical substrate but also by modulating the expression, organization, and activation of the relevant intracellular proteins, as well as by modulating the expression and organization of receptors for soluble factors in the extracellular environment which also influence cell motility. The additional potential avenue of mechanicochemical signaling initiated by cytoskeletal rearrangement awaits further investigation.

Animals↗
PubMed2001

Environmental factors of temperature, humidity, serum accumulation, and cell seeding increase colon cancer cell adhesion in vitro, with partial characterization of the serum component responsible for pressure-stimulated adhesion.

Physical characteristics of surgical wounds and viable tumor cells shed may differ between open and laparoscopic procedures. Because environmental factors may vary between the laparoscopic milieu and that of open surgical procedures, we sought to characterize the effect of these factors on tumor cell adhesion, an early step in the process of wound implantation. Human SW620 colon cancer cells were placed in matrix-precoated dishes for 30 min at concentrations of 90,000-540,000 cells/well, at 25-37 degrees C, in the native state of the matrix proteins and after drying for 60 min, and in 0-10% serum. As increased pressure has previously been reported to stimulate colon cancer cell adhesion synergistically with serum, we then further partially characterized the serum components responsible for this potentiating effect. The number of adherent cells varied linearly with cells seeded. Adhesion was temperature-dependent, and also was dependent on the matrix conformation. Less adhesion occurred to dry matrix proteins. Serum dose-dependently potentiated SW620 pressure-stimulated adhesion, with a maximal increase in adhesion compared with ambient pressure conditions at 5% serum concentration. Heat inactivating the serum at 60 degrees C for 30 min ablated the effect. Filtration to remove molecules over 10 kDa produced no change in adhesion relative to ambient conditions, but filtration to 100 kDa preserved the serum effect. When the serum was passed over a gelatin-Sepharose column, which binds numerous proteins including fibronectin, the serum effect was lost. Addition of fibronectin to serum-free media did not reconstitute the effect. The environmental factors of warm temperature, moisture, and serum accumulation may contribute to increased colon cancer cell adhesion. However, the most important determinant of malignant adhesion to surgical wounds, laparoscopic or open, is likely to be the size of the tumor cell inoculum. Pressure stimulation of colon cancer cell adhesion is potentiated by heat-labile serum components of molecular weight 10-100 kDa which bind gelatin-Sepharose, and is not fibronectin alone. Irrigating serum from surgical wounds may decrease tumor implantation.

Blood Proteins↗
PubMed2001

Complications of endoscopy.

BACKGROUND: Although most gastrointestinal endoscopic procedures are performed by gastroenterologists, surgeons often assist in the management of patients with complications. This review provides an introduction to the incidence, prevention, and treatment of complications that may occur after upper endoscopy, colonoscopy, percutaneous endoscopic gastrostomy, and endoscopic retrograde cholangiopancreatography. METHODS: Systematic review of the literature. RESULTS: Preprocedural complications include medication effects and adverse effects of bowel preparation. Major procedural complications consist primarily of perforation and hemorrhage. Percutaneous endoscopic gastrostomy tube placement may be complicated by fistula and obstruction. There is also a risk of infectious disease transmission, both to and from the patient. CONCLUSIONS: Endoscopy, like all invasive procedures, carries significant potential risks for the patient. In practiced hands, and with awareness of the problems that may arise, many complications may be avoided and others successfully managed.

Cholangiopancreatography, Endoscopic Retrograde↗
PubMed2001

Short chain fatty acids differentially modulate cellular phenotype and c-myc protein levels in primary human nonmalignant and malignant colonocytes.

Short chain fatty acids may protect colonic mucosa against neoplastic transformation by modulating colonocyte phenotype, DNA synthesis, and c-myc levels. To test this hypothesis, nonmalignant and malignant human colonocytes were isolated from surgical specimens and treated with 10 mM acetate, propionate, or butyrate. Markers of cellular phenotype, DNA synthesis, and c-myc protein levels were assayed by alkaline phosphatase and dipeptidyl dipeptidase IV activities, [3H]thymidine labeling, and western blotting, respectively. Butyrate, in particular, exerted discordant effects on alkaline phosphatase (P < 0.05), and c-myc levels (P < 0.05, N > or = 6) in nonmalignant and malignant human colonocytes. DPDD was unaffected by any of the short chain fatty acids tested. [3H]Thymidine labeling was differentially stimulated by short chain fatty acids in both cell types and greater DNA synthesis rates were observed in malignant colonocytes (P < 0.005, N = 16). These data suggest that in vitro, butyrate, in particular, may differentially modulate phenotype, DNA synthesis, and c-myc in nonmalignant and malignant human colonocytes.

Aged↗
PubMed2001

Differential dietary effects on colonic and small bowel neoplasia in C57BL/6J Apc Min/+ mice.

The effects of fiber on colon cancer are controversial. Twenty 5-week old C57BL/6J Apc Min/+ mice were fed for 60 days with a commercial mouse diet (Teklad LM-485) and eight semidefined diets containing 5-10% various fibers and 20% soybean oil. Ten additional C57BL/6J congenic litter-mates were fed each diet to assay colonic SCFA. SCFA, stool bulk, and colonic tumor incidence differed only slightly among the semidefined diets despite variations in fiber content and source. However, food consumption, caloric intake, stool bulk, and SCFA were substantially increased by the Teklad diet compared with all other groups. The Teklad diet significantly increased the number of mice with colonic tumors, average number of tumors/mouse, total tumor burden, colonic atypical hyperplasia, and small bowel tumors. Mice fed high-fat, no-fiber diets had more small bowel tumors (29.8 +/- 3.1) than mice fed diets with fiber (8.2 +/- 2.1) or with low fat and no fiber (18.1 +/- 3.4) (P < 0.05 for each group). These studies suggest that fat predisposes to and fiber protects against small bowel tumors but not colon tumors in these mice. Thus, diets high in fiber or yielding high colonic luminal SCFA may not necessarily protect against colonic cancer. Furthermore, the effects of dietary fiber in Teklad appear overshadowed by some other biologically active factors in this animal model.

Animals↗
PubMed2001

Effect of nabumetone and aspirin on colonic mucosal bleeding time.

BACKGROUND: The management of patients taking aspirin or non-steroidal anti-inflammatory drugs (NSAIDs) who require colonoscopy remains controversial because of concerns over bleeding after biopsy or polypectomy. AIM: To determine whether patients using the NSAID nabumetone, a non-acidic prodrug with mixed activity against cyclooxygenase-1 (COX-1) and COX-2, exhibited prolonged mucosal bleeding times and how this might compare with mucosal bleeding times in patients using aspirin. METHODS: We assessed triplicate mucosal bleeding times in patients undergoing screening flexible sigmoidoscopy. We compared 90 patients who had taken no aspirin or NSAIDs within the previous 2 weeks, to 60 patients who had received nabumetone 1 g b.d. by mouth for the previous 2 weeks, and 30 patients who had taken 325 mg aspirin daily for the previous 2 weeks. In each case, the investigator performing the study was blinded to the patient's medication. RESULTS: Mucosal bleeding times did not differ significantly among control or nabumetone-using patients. However, the patients receiving aspirin exhibited significant prolongation. Mucosal bleeding time correlated statistically significantly, but weakly, with skin bleeding time. CONCLUSIONS: Nabumetone does not appear to prolong mucosal bleeding time after mucosal pinch biopsy, and skin bleeding time does not reliably screen for prolonged mucosal bleeding time.

Administration, Oral↗
PubMed2001

Short-chain fatty acids inhibit invasive human colon cancer by modulating uPA, TIMP-1, TIMP-2, mutant p53, Bcl-2, Bax, p21 and PCNA protein expression in an in vitro cell culture model.

High intakes of dietary fiber or resistant starches have been associated with a lower incidence of colon cancers. Because short-chain fatty acids (SCFA) such as butyrate are produced in the colonic lumen by the bacterial fermentation of dietary fibers and resistant starches, we hypothesized that SCFA may inhibit the development of invasive human colon cancers. To test this hypothesis, primary human invasive colonocytes were isolated from fresh surgical specimens and treated with 0.01 mol/L acetate, propionate or butyrate; cell invasion, cell adhesion, F-actin polymerization, urokinase plasminogen activator (uPA), tissue inhibitor matrix metalloproteinase (TIMP)-1, TIMP-2 and mutant p53, Bcl-2, Bax, p21 and proliferating cell nuclear antigen (PCNA) protein expression levels were examined. Although each of the SCFA tested significantly reduced primary cell invasion, butyrate was the most potent, inhibiting primary invasive human colon cancer invasion by 54% (P < 0.0001). The effects of SCFA on primary cell invasion appeared to be independent of cell adhesion and F-actin polymerization but dependent on the inhibition of uPA (P < 0.05) and the stimulation of TIMP-1 and TIMP-2 activities (P < 0.05). Protein expression levels of mutant p53, p21, Bax, Bcl-2 and PCNA were significantly altered by each of the SCFA tested (P < 0.05). These data indicate that SCFA inhibit invasive human colon cancer by modulating proteolytic uPA and antiproteolytic TIMP-1 and TIMP-2 activities, but their mechanisms of action on tumor suppression, apoptosis and growth arrest may differ.

Actins↗
PubMed2001

Integrin and FAK-mediated MAPK activation is required for cyclic strain mitogenic effects in Caco-2 cells.

Rhythmic strain stimulates Caco-2 proliferation. We asked whether mitogen-activated protein kinase (MAPK) activation mediates strain mitogenicity and characterized upstream signals regulating MAPK. Caco-2 cells were subjected to strain on collagen I-precoated membranes or antibodies to integrin subunits. Twenty-four hours of cyclic strain increased cell numbers compared with static conditions. MAPK-extracellular signal-regulated kinase (ERK) kinase inhibition (20 microM PD-98059) blocked strain mitogenicity. p38 Inhibition (10 microM SB-202190) did not. Strain rapidly and time-dependently activated focal adhesion kinase (FAK), paxillin, ERK1 and 2, and p38 on collagen. c-Jun NH(2)-terminal kinase (JNK)1 and 2 exhibited delayed activation. Similar activation occurred when Caco-2 cells were subjected to strain on a substrate of functional antibody to the alpha2-, alpha3-, alpha6-, or beta1-integrin subunits but not on a substrate of functional antibody to the alpha5-subunit. FAK inhibition by FAK397 transfection blocked ERK2 and JNK1 activation by in vitro kinase assays, but pharmacological protein kinase C inhibition did not block ERK1 or 2 activation by strain. Strain-induced ERK signals mediate strain's mitogenic effects and may require integrins and FAK activation.

Caco-2 Cells↗
PubMed2000

Collagen IV-dependent ERK activation in human Caco-2 intestinal epithelial cells requires focal adhesion kinase.

Integrin-initiated extracellular signal-regulated kinase (ERK) activation by matrix adhesion may require focal adhesion kinase (FAK) or be FAK-independent via caveolin and Shc. This remains controversial for fibroblast and endothelial cell adhesion to fibronectin and is less understood for other matrix proteins and cells. We investigated Caco-2 intestinal epithelial cell ERK activation by collagen I and IV, laminin, and fibronectin. Collagens or laminin, but not fibronectin, stimulated tyrosine phosphorylation of FAK, paxillin, and p130(cas) and activated ERK1/2. Shc, tyrosine-phosphorylated by matrix adhesion in many cells, was not phosphorylated in Caco-2 cells in response to any matrix. Caveolin expression did not affect Caco-2 Shc phosphorylation in response to fibronectin. FAK, ERK, and p130(cas) tyrosine phosphorylation were activated after 10-min adhesion to collagen IV. FAK activity increased for 45 min after collagen IV adhesion and persisted for 2 h, while p130(cas) phosphorylation increased only slightly after 10 min. ERK activity peaked at 10 min, declined after 30 min, and returned to base line after 1 h. Transfection with FAK-related nonkinase, but not substrate domain deleted p130(cas), strongly inhibited ERK2 activation in response to collagen IV, indicating Caco-2 ERK activation is at least partly regulated by FAK.

Caco-2 Cells↗
PubMed2000

Matrix-specific FAK and MAPK reorganization during Caco-2 cell motility.

We have previously reported that Caco-2 cell motility redistributes FAK, paxillin, and activates p38. However, the subcellular organization of these intracellular signals during cell migration is unclear. We, therefore, investigated the organization of actin, FAK, paxillin, and activated ERK and activated p38 during Caco-2 motility across collagen I, fibronectin, laminin, and tissue culture treated glass. Differential density seeding generated homogeneous static and migrating populations. Expression of actin, FAK, paxillin, phospho-ERK, and phospho-p38 were examined by immunofluorescent staining in static and motile cells. Actin was concentrated toward the peri-nuclear central area of cells migrating on matrix proteins studied. Actin immunoreactivity was decreased in the leading edge of lamellipodia. FAK immunoreactivity was weaker in migrating cells than in static cells on the same matrix. FAK was expressed along cell-cell contacts of both cell populations, but absent in migrating lamellipodia of matrix-cultured cells. Paxillin staining was diffuse in static cells but organized toward migrating lamellipodia in a radial manner. Like FAK, phosphorylated ERK was expressed in the central region of migrating cells but was dramatically decreased at areas of cell-cell contact and free lamellipodia. Fibronectin exerted the greatest effect on ERK activation in all matrix proteins studied. In contrast, phosphorylated p38 staining was stronger in migrating cells on matrix than in static cells on the same matrix. Phosphorylated p38 was expressed in the nuclear of migrating cells and disappeared in the cell-cell contact side and free lamellipodia. Interestingly, the reorganization of these proteins was distinctly different on tissue culture treated glass without a physiologic matrix substrate. For instance, FAK staining increased rather than decreased in motile cells on plastic, and lamellipodial FAK staining could be discerned. Matrix may influence Caco-2 biology during migration not only by triggering intracellular phosphorylation events but also by reorganizing the cytoskeleton and the subcellular localization of these intracellular signals.

Actins↗
PubMed2000

Mitogen-activated protein phosphorylation in endothelial cells exposed to hyperosmolar conditions.

The effect of hyperosmolarity on the induction of the mitogen-activated protein kinases (MAPK) was studied in bovine aortic endothelial cell (EC). Different types of agents were used to differentiate the effects of osmolarity from other variables. Hypertonic treatment with physiologically relevant levels of NaCl (350 mOsm/kg H(2)O) significantly increased the level of expression of p38 within 2 min, and ERK-1/2 and JNK after 10 min. The inductions peaked between 30 and 60 min and returned to baseline levels within 2 h. A similar pattern of induction occurred with ionic contrast agent. p38 induction by glucose and mannitol showed a similar pattern, although the level of ERK-1/2 phosphorylation was not as robust, and JNK was not induced by glucose. Urea did not affect the level of induction of the MAPK isoforms. It is concluded that MAPK plays an important role in hyperosmolality-induced signal transduction. Different osmotic agents induce MAPK expression differently. No MAPK induction with urea implies that cell shrinkage may be an important component of hyperosmolality-induced MAPK phosphorylation.

Animals↗
PubMed2000

Effects of increased ambient pressure on colon cancer cell adhesion.

Forces such as strain modulate intestinal epithelial biology. Shear and pressure influence other cells. The effects of pressure on human colon cancer cells are poorly understood. Increasing ambient pressure for 30 min by 15 mm Hg over atmospheric stimulated adhesion to matrix proteins of four human colon cancer cell lines and primary cells from three human colon cancers, but not bovine aortic smooth-muscle cells. This effect was energy dependent and cation dependent (blocked by azide and chelation), accompanied by tyrosine phosphorylation of intracellular proteins including focal adhesion kinase, and blocked by tyrosine kinase inhibition (genistein, tyrphostin, and erbstatin) and a functional antibody to the beta1 integrin subunit. Although pressure stimulated adhesion even in a balanced salt solution, baseline and pressure-stimulated adhesion were each substantially diminished in the absence of serum. These data suggest that relatively low levels of increased pressure may stimulate malignant colonocyte adhesion by a cation-dependent beta1-integrin-mediated mechanism, perhaps via focal adhesion kinase-related tyrosine phosphorylation. In addition to elucidating another aspect of physical force regulation of colonocyte biology, these findings may be relevant to the effects of increased pressure engendered by colonic peristalsis, surgical manipulation, or laparoscopic surgery on colon cancer cell adhesion.

Animals↗
PubMed2000

Human caco-2 motility redistributes FAK and paxillin and activates p38 MAPK in a matrix-dependent manner.

The signals involved in restitution during mucosal healing are poorly understood. We compared focal adhesion kinase (FAK) and paxillin protein and phosphorylation, extracellular signal-regulated kinase (ERK) 1, ERK2, and p38 activation, as well as FAK and paxillin organization in static and migrating human intestinal Caco-2 cells on matrix proteins and anionically derivatized polystyrene dishes (tissue culture plastic). We also studied effects of FAK, ERK, and p38 blockade in a monolayer-wounding model. Compared with static cells, cells migrating across matrix proteins matrix-dependently decreased membrane/cytoskeletal FAK and paxillin and cytosolic FAK. Tyrosine phosphorylated FAK and paxillin changed proportionately to FAK and paxillin protein. Conversely, cells migrating on plastic increased FAK and paxillin protein and phosphorylation. Migration matrix-dependently activated p38 and inactivated ERK1 and ERK2. Total p38, ERK1, and ERK2 did not change. Caco-2 motility was inhibited by transfection of FRNK (the COOH-terminal region of FAK) and PD-98059, a mitogen-activated protein kinase-ERK kinase inhibitor, but not by SB-203580, a p38 inhibitor, suggesting that FAK and ERK modulate Caco-2 migration. In contrast to adhesion-induced phosphorylation, matrix may regulate motile intestinal epithelial cells by altering amounts and distribution of focal adhesion plaque proteins available for phosphorylation as well as by p38 activation and ERK inactivation. Motility across plastic differs from migration across matrix.

Caco-2 Cells↗
PubMed2000

Alpha integrin subunits regulate human (Caco-2) intestinal epithelial proliferation and phenotype.

BACKGROUND/AIMS: Cell-matrix interactions influence intestinal epithelial biology, but the whether specific integrin heterodimers exert different effects is unclear. METHODS: We used functional antibodies to investigate effects of the alpha2, alpha3, alpha5, and alpha6 integrin subunits on proliferation and differentiation of human intestinal Caco-2 cells on laminin. Cells seeded onto laminin-coated inserts in defibronectinized medium were treated with functional antibodies or normal IgG for 72 hrs and proliferation, alkaline phosphatase and dipeptidyl dipeptidase specific activity were measured. RESULTS: Caco-2 adhesion to antibody to each alpha-integrin subunit stimulated tyrosine phosphorylation of Focal Adhesion Kinase and paxillin, suggesting that these antibodies intiate integrin-related tyrosine signalling. Proliferation was inhibited by anti-alpha2 and anti-alpha3, but stimulated by anti-alpha6. Alkaline phosphatase and dipeptidyl dipeptidase specific activity were promoted by alpha2 blockade but decreased after a6 blockade. Proliferative blockade using mitomycin C or hydroxyurea prevented the effects of alpha2 ligation on differentiation, but the decrease in alkaline phosphatase specific activity observed after a6 integrin subunit blockade was preserved even after proliferative blockade. CONCLUSION: lntegrin heterodimers modulate human Caco-2 intestinal epithelial biology on laminin in an alpha-subunit specific manner. The different effects of anti-alpha2 and anti-alpha6 may reflect competitition by these antibodies with integrin subunit interactions with laminin as well as initiation of their own signals or different functions for the alpha6 integrin subunit

Antibodies↗
PubMed1998

Mechanical strain rapidly redistributes tyrosine phosphorylated proteins in human intestinal Caco-2 cells.

Repetitive strain stimulates proliferation and modulates differentiation in human Caco-2 intestinal epithelial cells via tyrosine kinase activity. We therefore sought to characterize strain modulation of tyrosine phosphorylation in Caco-2 cells. Immunoblotting for phosphotyrosine demonstrated that repetitive strain (10 cpm, 10% strain) rapidly increased tyrosine phosphorylation of 125-, 70-, 60-, and 50-kDa bands in the soluble fraction by 94+/-31, 145+/-21, 365+/-46, and 1240+/-240%, respectively (p<0.05, n=4). However, strain decreased tyrosine phosphorylated band intensity of the 125-, 70-, 60-, and 50-kDa proteins in the particulate fraction by 81+/-17, 70+/-23, 79+/-7, and 59+/-23%, respectively (p<0.05, n=4). The decreased band intensity in the particulate fraction was not due to decreased tyrosine kinase activity because strain equally increased tyrosine kinase activity in both soluble and particulate fractions. Cyclic strain at a physiologically relevant amplitude and frequency appears to modulate the subcellular distribution of tyrosine phosphorylated proteins in human Caco-2 intestinal cells.

Caco-2 Cells↗