SEARCH · PubMed Health

Results for “Prostatic Secretory Proteins”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 55 records · Page 3Linked to original sources

PubMed1992

Hormonal modulation of biosynthesis of prostatic specific antigen, prostate specific acid phosphatase and prostatic inhibin peptide.

Hormonal modulation of in vitro biosynthesis of three prostatic secretory proteins, prostate specific acid phosphatase (PSAP), prostate specific antigen (PSA) and prostatic inhibin peptide (PIP) by human benign hyperplasia (BPH) tissue was studied. LH and inhibins caused increase in the synthesis of all three proteins whereas FSH enhanced the synthesis of PIP and PSA only but decreased PSAP synthesis. Prolactin and thyroid releasing hormone decreased synthesis of PIP and PSAP. However, PSA synthesis was enhanced by TRH and was decreased by prolactin. Estradiol caused significant increase in PSA and PSAP but no discernible changes in PIP synthesis were noticed. Testosterone caused an increase in PIP, PSA and PSAP. These data indicate that biosynthesis of PIP, PSA and PSAP by BPH tissue is under multihormonal regulation.

Acid Phosphatase↗

PubMed1998

Evaluation of seminal plasma parameters in patients with chronic prostatitis or leukocytospermia.

Though detailed cytological and microbiological diagnostic procedures are routinely carried out in male genital tract infection, the correct diagnosis and localization of inflammation or infection is often difficult. In this prospective study, the relevance of the seminal plasma markers PMN elastase, complement C3, CRP, fructose, PSP 94, PSA, and alpha-glucosidase was investigated in 13 patients with chronic prostatitis, 31 patients with significant leukocytospermia, and 58 patients with non-inflammatory diseases (controls). Statistically relevant results were obtained for PMN elastase when comparing chronic prostatitis with controls, leukocytospermia with controls (P < 0.001) and chronic prostatitis with leukocytospermia (P < 0.05); for complement C3 chronic prostatitis and leukocytospermia vs. controls (P < 0.05) and for fructose/ejaculate leukocytospermia vs. controls (P < 0.05). No statistically relevant differences were found for C-reactive protein, alpha-glucosidase, PSA and prostatic secretory protein (PSP 94). To delimit genital tract inflammation from non-inflammatory patients, cutpoint levels for PMN elastase of 230 ng ml-1 and for C3c of 0.01 g l-1 were suggested. PMN elastase was shown to possess the strongest discriminating power. The assessment of a cutpoint for fructose to indicate seminal vesicle dysfunction is not possible as the significance level is weak (P < 0.05).

Adolescent↗

PubMed1996

Induction of seminal vesicle morphogenesis from dog epididymal epithelium.

A number of carnivores, including the dog, do not have seminal vesicles (SVs). They have been induced experimentally by heterotypic recombination of adult dog epididymal epithelium with mesenchyme of neonatal rat SV and allowed to grow for 4 weeks under the renal capsule of male athymic nude mice. The induced SVs bore a striking similarity to rat SV both histologically and ultrastructurally. However, they secreted proteins which were different from those in the rat SV and reacted negatively to antibodies specific to rat SV secretory proteins and dog prostate secretory proteins. The results strongly suggested that the glands induced from dog epididymal epithelium were likely to be "dog" SVs.

Animals↗

PubMed2003

Mouse PSP94 expression is prostate tissue-specific as demonstrated by a comparison of multiple antibodies against recombinant proteins.

Prostate tissue-specific gene expression is crucial for driving potentially therapeutic genes to target specifically to the prostate. Prostate secretory protein of 94 amino acids (PSP94), also known as beta-MSP (microseminoprotein), is one of the three most abundant secretory proteins of the prostate gland, and is generally considered to be prostate tissue-specific. We have previously demonstrated that the expression of the rat PSP94 gene is strictly prostate tissue-specific by an antibody against a recombinant rat PSP94. In order to study prostate targeting utilizing the PSP94 gene in a mouse pre-clinical experimental model, we need to establish antibodies against mouse PSP94 to confirm if it is prostate tissue-specific as well. In this study, firstly we raised a polyclonal antibody against a recombinant glutathione-S-transferase- (GST-) mouse mature form of PSP94. However, it showed very poor immunoreactivity against prostate tissue PSP94 as tested in Western blotting experiments. Neither antibodies against rat PSP94 nor mouse PSP94 showed significant cross-reactivity. Thus a second antibody was established against a recombinant mouse mature PSP94 containing N-terminal polyhistidines, and stronger immunoreactivity against mouse prostate tissue PSP94 was identified in Western blotting experiments. Both of these antibodies showed immunohistochemical reactivity, while the latter showed stronger reactivity in IHC when tested with different fixatives. By studying tissue distribution, we demonstrated that, as with rat PSP94, mouse PSP94 is strictly prostate tissue-specific in experiments of both Western blotting and immunohistochemistry (IHC). This conclusion was also derived from a comparison among antibodies against human, rat, and mouse PSP94, showing very different immunoreactivities in Western blotting and IHC. Finally, a competitive assay between different species was performed. We demonstrated that antibodies against PSP94 from different species (human, primate, rodents) have poor cross-reactivities. These observations also indicate that the PSP94 gene is a rapidly evolving gene in all species. Results from this study have led to the possibility of utilizing PSP94 as a targeting agent specifically to the prostate in a mouse experimental model.

Animals↗

PubMed1998

An expressed-sequence-tag database of the human prostate: sequence analysis of 1168 cDNA clones.

The human prostate is a complex glandular organ with functional development under hormonal regulation. Diseases of the prostate result in significant morbidity and mortality in the form of benign prostatic hypertrophy and prostate adenocarcinoma. The characterization of the molecular framework of the human prostate at the level of expressed genes will facilitate the understanding of normal and pathological prostate biology. The purposes of this study were to acquire an initial assessment of the qualitative and quantitative diversity of gene expression in the normal human prostate and to determine the extent that genes with prostate-restricted expression can be assessed using an expressed sequence tag approach. We have constructed a directional cDNA library from normal adult human prostate tissue and partially sequenced the 5' end of 1168 randomly selected cDNA clones, resulting in more than 400 kb of DNA sequence. Homology searches of the sequenced cDNAs against the GenBank and dbEST databases revealed that 43% of the sequences are identical to human genes whose functions are known, 5% are similar but not identical to known genes in humans or lower organisms, 5% match the mitochondrial genome, 9% are composed of interspersed DNA repeats, 30% are homologous to sequences in the dbEST database without a described function, and 6% are novel sequences. A total of 780 distinct species were identified. In addition to the 74 novel transcripts, 4 genes, prostate-specific antigen (PSA), prostate secretory protein (PSP), prostate acid phosphatase (PAP), and human glandular kallekrein 2 (HK2), have no homologous sequences in the databases that originate from sources other than prostate and thus may represent genes with prostate-restricted expression. Sequences matching PSA, PSP, and PAP each accounted for > 1% of the total ESTs and represent highly abundant transcripts, correlating with the abundance of these proteins in the prostate gland. No novel transcripts were represented by more than one EST and thus are expressed at levels much lower than the known prostate-specific genes.

Adult↗

PubMed1990

Expression of Zn-alpha 2-glycoprotein and PSP-94 in prostatic adenocarcinoma. An immunohistochemical study of 88 cases.

Zn-Alpha 2-Glycoprotein (Zn-Alpha 2-GP) and prostatic secretory protein of 94 amino-acids (PSP-94) were recently isolated from the human prostate. Their expression in benign and malignant well-differentiated and poorly differentiated components of 88 prostates with prostatic adenocarcinomas, and in 25 metastases, was evaluated using polyclonal antibodies developed against these antigens. Zn-Alpha 2-GP was present in benign hyperplastic glands in 91.1% of cases, but in only 40.7% (poorly differentiated component) to 48.5% (well-differentiated component) of prostatic adenocarcinomas, and in 8% of metastases. The expression of PSP-94 was present in 89.3% of benign hyperplastic glands, but in only 50% (well-differentiated adenocarcinoma component) to 57.3% (poorly differentiated component) of prostatic adenocarcinomas and 28% of metastases. The expression of these proteins by the tumor was unrelated to the initial stage and the tumor grade. Because of their low frequency in prostatic adenocarcinomas, especially in metastases, Zn-Alpha 2-GP and PSP-94 appear to have a limited diagnostic usefulness. Further studies are needed, however, to explore other clinical applications of these two new prostatic secretory proteins.

Adenocarcinoma↗

PubMed2003

Transcriptional silencing of zinc finger protein 185 identified by expression profiling is associated with prostate cancer progression.

We profiled the expression of genes in benign and untreated human prostate cancer tissues using oligonucleotide microarrays. We report here 50 genes with distinct expression patterns in metastatic and confined tumors (Gleason score 6 and 9; lymph node invasive and noninvasive). Validation of expression profiles of 6 genes by quantitative PCR revealed a strong inverse correlation in the expression of zinc finger protein 185 (ZNF185), bullous pemphigoid antigen gene (BPAG1), and prostate secretory protein (PSP94) with progression of prostate cancer. Treatment of prostate cancer cell lines with 5-aza-2'-deoxycytidine (5-Aza-CdR), an inhibitor of DNA methylation, restored ZNF185 expression levels. Moreover, methylation-specific PCR confirmed methylation of the 5'CpG islands of the ZNF185 gene in all of the metastatic tissues and 44% of the localized tumor tissues, as well as in the prostate cancer cell lines tested. Thus, transcriptional silencing of ZNF185 by methylation in prostate tumor tissues implicates the ZNF185 gene in prostate tumorigenesis.

Aged↗

PubMed1986

Carcinogen-binding proteins in the rat ventral prostate: specific and nonspecific high-affinity binding sites for benzo(a)pyrene, 3-methylcholanthrene, and 2,3,7,8-tetrachlorodibenzo-p-dioxin.

The polychlorinated dibenzodioxin [3H]-2,3,7, 8-tetrachlorodibenzo-p-dioxin (TCDD) and the carcinogens [3H]benzo(a)pyrene and [3H]-3-methylcholanthrene bound to saturable binding sites in cytosol from the rat ventral prostate. Analysis of equilibrium binding parameters in diluted cytosol preparations indicated an apparent Kd of approximately 2 nM and a binding capacity of approximately 1 nmol/mg cytosolic protein, corresponding to approximately 5% of the total protein content. However, gel permeation chromatography analysis as well as velocity sedimentation analysis on sucrose gradients of [3H]TCDD-labeled rat prostatic cytosol indicated binding of [3H]TCDD to two discrete species. These analyses indicated a sedimentation coefficient of 3.6-3.8S, a Stokes radius of 25-28 A, and a calculated relative molecular weight of 42,000-45,000 for the most abundant binding species. The other binding species sedimented at 4-5S under high ionic strength conditions and at 8-10S under low ionic strength conditions and had a Stokes radius of approximately 60 A, a relative molecular weight of approximately 100,000 and an estimated concentration of 5-20 fmol/mg cytosolic protein. Binding of [3H]TCDD to this species was displaceable by a 200-fold M excess of 2,3,7,8-tetrachlorodibenzofuran. Therefore, this species was tentatively identified as the TCDD receptor. The properties of the high-capacity binder of [3H]TCDD were found to be similar to the characteristics of a protein previously purified from the rat ventral prostate, prostatic secretory protein, which binds androgens as well as estramustine, a nitrogen mustard derivative of estradiol. The binding of estramustine to diluted prostatic cytosol was shown to be competitively inhibited by 2,3,7,8-tetrachlorodibenzofuran. Moreover, purified prostatic secretory protein bound [3H]TCDD, [3H]benzo(a)pyrene, as well as [3H]-3-methylcholanthrene. It is suggested that binding to this protein is responsible for the high-binding capacity of carcinogens in cytosol from the rat ventral prostate.

Animals↗

PubMed2000

PSP94 (or beta-microseminoprotein) is a secretory protein specifically expressed and synthesized in the lateral lobe of the rat prostate .

BACKGROUND: Prostatic secretory protein of 94 amino acids (PSP94), also called beta-microseminoprotein, is a small, nonglycosylated protein, rich in cysteine residues. It was first isolated as a major protein from human seminal plasma. Subsequently, its homologous proteins were identified, and their cDNAs or genes have been cloned in primates, pigs, and rodents. METHODS: The present study investigated the expression pattern of PSP94 in the normal Noble rat prostate gland by nonradioactive in situ hybridization, Northern blotting, RT-PCR, Western blotting, and immunohistochemistry. Its expression in the mouse prostate gland was also examined by in situ hybridization. RESULTS: The results of in situ hybridization, and Northern and Western blot analyses, showed that the expression of rat PSP94 was prostate-specific. It was highly expressed in the lateral prostatic lobe, moderate in the dorsal lobe, weak in the coagulating gland, and negative in the ventral lobe and seminal vesicle. Its specific expression in the rat prostate gland was further confirmed by RT-PCR analysis of prostatic and nonprostatic organ tissues. Its mRNA transcripts were not detected in the urinary, digestive, and respiratory tracts, male and female reproductive organs, muscles, brain, and kidney. Its molecular mass was estimated to be 14.5 kDa by Western blotting. Similar prostate-specific expression of PSP94 was also observed by in situ hybridization in the lateral lobe, but not in the dorsal and ventral lobe, of the mouse prostate gland. CONCLUSIONS: Rat PSP94 is a major secretory protein highly expressed and synthesized by the lateral lobe of both rat and mouse prostate glands, and moderately expressed in the dorsal lobe of the rat prostate gland.

Animals↗

PubMed1982

High resolution analysis of human prostatic fluid by two-dimensional electrophoresis.

High-resolution two-dimensional electrophoresis has been used to resolve the major protein components of human prostatic fluid. Samples taken from individuals ranging in age from 19 to 74 years show ten major proteins that are consistently present in the fluids examined. Seven major proteins appear to have age-dependent patterns of synthesis and accumulation in the prostatic fluid. A major protein in the human fluid has electrophoretic properties similar to the glycosylated component of the rat ventral prostate secretory protein known as prostatic binding protein, prostatein, or estramustine binding protein. The isoelectric point/molecular weight of the human protein is 6.0/17,000 compared with 5.6/13,000 for the rat protein. Protein patterns from benign prostatic hyperplasia cases were not dramatically different from the normal patterns.

Adult↗

PubMed2006

Evidence of a novel biomarker, alphas1-Casein, a milk protein, in benign prostate hyperplasia.

Benign prostate hyperplasia (BPH) is a common disease in elderly men. Although it is a non-malignant disease, it has a significant detrimental impact on the quality of life in patients with late-stage disease. Owing to the lack of specific markers, diagnosis of early-stage BPH has been proven unsuccessful. Recently, using two-dimensional electrophoresis, we identified a group of prostatic secretory proteins that are specifically produced by BPH cells (Xu et al., Electrophoresis 2003; 24: 1311). In this study, we investigated the potential diagnostic value of one of the secretory proteins, alphas1-Casein, in BPH by inmmunohistological staining of normal, BPH and prostate cancer tissues. We found that 90% (20 out of 22) of BPH tissues showed moderate to strong alphas1-Casein protein expression whereas none of the normal tissues (0 out of 10) and less than 10% of the prostate cancer tissues (3 out of 30) showed similar staining intensity. Our results suggest that alphas1-Casein may be a potential biomarker for early identification of BPH patients.

Adenocarcinoma↗

PubMed2006

Quantitative determination of lobe specificity of mRNA expression of androgen-dependent genes in the rat prostate gland.

The rodent prostate has a complex structure, consisting of a ventral prostate (VP), lateral prostate (LP), dorsal prostate (DP) and anterior prostate (AP), and most studies so far have focused on the VP. Androgen-responsive prostatic secretory proteins, such as prostatein and kallikreins, are mainly produced in the VP, but others are abundant in the LP and DP, though little is known about differences of androgen regulation among the different lobes. Here, the mRNA expression levels of some representative androgen-responsive genes, including those encoding prostatic secreted proteins, were quantitatively determined in each of the prostatic lobes of intact rats and castrated rats treated with testosterone alone or plus flutamide. The results show that the transcriptional regulation of prostatic secretory proteins differs greatly among lobes, generally being more tightly regulated in the VP. A number of growth factor mRNAs were differentially expressed in separate lobes and were regulated by testosterone in a lobe-specific manner. Lobe-specific regulation by androgen was also found for other genes, including the DAD-1 and calreticulin genes. Thus, hormone-dependent transcriptional regulation of prostate genes differs among lobes, and there is also interlobar diversity of basal mRNA expression levels.

Androgens↗

PubMed1991

Rapid evolution of prostatic protein PSP94 suggested by sequence divergence between rhesus monkey and human cDNAs.

Comparison of the protein coding region of mRNA for the prostatic secretory protein PSP94 in human (hPSP94) with that in rhesus monkey (rmPSP94) indicates that, for the most part, its sequence has evolved with few constraints and at a relatively fast rate. Interestingly, half of the 22 residue differences between the two species involve charge changes, reflected by the acidic pI (5.4) of hPSP94 and the basic pI (10.6) of rmPSP94. However, the 10 cysteines and 5 of the 6 prolines of PSP94 were unaffected, suggesting that the three-dimensional conformations of the human and the monkey proteins may be similar. Rapid evolution of this gene might explain the apparent absence in nonprimates of homologous sequences detectable by hybridization.

Amino Acid Sequence↗

PubMed2006

Inhibition of MMP-9 secretion by the anti-metastatic PSP94-derived peptide PCK3145 requires cell surface laminin receptor signaling.

PCK3145 is a synthetic peptide corresponding to amino acids 31-45 of prostate secretory protein 94 which can reduce experimental skeletal metastases and prostate tumor growth. These anti-metastatic and anti-tumoral effects of PCK3145 are partially explained by the in-vivo and in-vitro decrease in matrix metalloproteinase (MMP)-9 extracellular levels through as yet unidentified molecular mechanisms of action. Gelatin zymography and immunoblots were used to monitor the levels of secreted MMP-9 from HT-1080 cells. Flow cytometry was used to monitor HT-1080 cell surface binding of FITC-labeled PCK3145 and biotin-labeled laminin. PCK3145-coated cell culture dishes were used to monitor cell adhesion. HT-1080 cell lysates were used for immunoblotting of HuR, extracellular signal-regulated protein kinase (ERK) and phospho-ERK. Total RNA was isolated and RT-PCR used to monitor HuR gene expression. We found that PCK3145 bound to the HT-1080 cell surface and that this binding rapidly triggered ERK phosphorylation that, ultimately, led to a reduction of secreted MMP-9. Laminin inhibited both cell surface binding and ERK phosphorylation by PCK3145. Overexpression of the 67-kDa laminin receptor led to an increased binding of the cells to PCK3145. HuR, a protein that can bind to and stabilize MMP-9 mRNA, was found to be downregulated by PCK3145. The mitogen-activated protein kinase/ERK (MEK) inhibitor PD98059 as well as native laminin and SIKVAV laminin-derived peptide prevented that downregulation. Our data suggest that PCK3145 rapidly triggers intracellular signaling through cell surface laminin receptors. This leads to decreased HuR expression and subsequent destabilization of MMP-9 transcripts. This is the first molecular evidence demonstrating the intracellular signaling and anti-metastatic mechanism of action of PCK3145 that leads to the inhibition of MMP-9 secretion.

Antigens, Surface↗

PubMed1998

Identification of binding proteins for PSP94 in human prostate adenocarcinoma cell lines LNCaP and PC-3.

BACKGROUND: Prostatic secretory protein of 94 amino acids (PSP94) is one of the predominant proteins found in human seminal fluid. Limited information is available regarding a physiological function for PSP94. An important step in the elucidation of this function is the determination of the mechanism of interaction of PSP94 with potential cellular targets. METHODS: Equilibrium binding assay was employed to demonstrate specific binding of biotinylated-PSP94 to the LNCaP and PC-3 cell lines. Binding proteins were partially purified by PSP94 affinity-chromatography from LNCaP, PC-3 cells, and prostate tissues. RESULTS: Binding of biotinylated-PSP94 to LNCaP and PC-3 cells was saturable and time and temperature dependent. The binding could be specifically competitively inhibited by unlabelled PSP94. Two types of PSP94 binding sites with distinct affinity (Kd) and density (Bmax) were determined by Scatchard analysis for each of the two cell lines. For the LNCaP cells, these values were Kd 1 = 0.75 nM and Bmax1 = 300 fmol/mg protein and Kd 2 = 4.5 nM, Bmax2 = 780 fmol/mg protein, respectively. Similar affinity and density results were obtained for PC-3 cells: Kd 1 = 0.83 nM, Bmax1 = 250 fmol/mg protein, and Kd 2 = 5.0 nM, Bmax2 = 700 fmol/mg. The binding of biotinylated-PSP94 to the LNCaP cells was competitively inhibited by the partially purified proteins. Analysis of these proteins SDS-PAGE showed three main bands and the molecular weights of these three bands were approximately 180, 100 and 60 kD, respectively. CONCLUSIONS: The data showed the presence of specific binding proteins to the PSP94 in LNCaP, PC-3 cells, and prostate tissue.

Adenocarcinoma↗

PubMed1985

The antigenic relatedness of proteins from human and simian prostate fluid.

Two-dimensional electrophoretic analysis of human prostate fluid reveals an abundant protein migrating to a molecular weight of 15 kD and an isoelectric point of 5.5. Polyclonal antibodies were raised specifically to microgram quantities of electrophoresed, excised, and eluted PSP15 (prostate secretory protein). Western immunoblot analysis using these antibodies showed they not only react to PSP15, but cross-react with simian prostate and human seminal fluid proteins of similar molecular weights. Two-dimensional gel immunoblots strongly suggest that the seminal protein and PSP15 are the same, thereby providing a more accessible source of the protein. The antibody to the human PSP15 cross-reacted with neither prostate fluid from the ventral lobe of the rat prostate nor the prostate fluid from the beagle dog.

Animals↗

PubMed2005

A PSP94-derived peptide PCK3145 inhibits MMP-9 secretion and triggers CD44 cell surface shedding: implication in tumor metastasis.

PURPOSE: PCK3145 is a synthetic peptide corresponding to amino acids 31-45 of prostate secretory protein 94, which can reduce experimental skeletal metastases and prostate tumor growth in vivo. Part of its biological action involves the reduction of circulating plasma matrix metalloproteinase (MMP)-9, a crucial mediator in extracellular matrix (ECM) degradation during tumor metastasis and cancer cell invasion. The antimetastatic mechanism of action of PCK3145 is however, not understood. EXPERIMENTAL DESIGN: HT-1080 fibrosarcoma cells were treated with PCK3145, and cell lysates used for immunoblot analysis of small GTPase RhoA and membrane type (MT)1-MMP protein expression. Conditioned media was used to monitor soluble MMP-9 gelatinolytic activity by zymography and protein expression by immunoblotting. RT-PCR was used to assess RhoA, MT1-MMP, MMP-9, RECK, and CD44 gene expression. Flow cytometry was used to monitor cell surface expression of CD44 and of membrane-bound MMP-9. Cell adhesion was performed on different purified ECM proteins, while cell migration was specifically performed on hyaluronic acid (HA). RESULTS: We found that PCK3145 inhibited HT-1080 cell adhesion onto HA, laminin-1, and type-I collagen suggesting the common implication of the cell surface receptor CD44. In fact, PCK3145 triggered the shedding of CD44 from the cell surface into the conditioned media. PCK3145 also inhibited MMP-9 secretion and binding to the cell surface. This effect was correlated to increased RhoA and MT1-MMP gene and protein expression. CONCLUSIONS: Our data suggest that PCK3145 may antagonize tumor cell metastatic processes by inhibiting both MMP-9 secretion and its potential binding to its cell surface docking receptor CD44. Such mechanism may involve RhoA signaling and increase in MT1-MMP-mediated CD44 shedding. Together with its beneficial effects in clinical trials, this is the first demonstration of PCK3145 acting as a MMP secretion inhibitor.

Fibrosarcoma↗

PubMed1989

Immunocytochemical localization and lectin-binding properties of the 22 kDa secretory protein from rat ventral prostate.

The distribution of the 22 kDa secretory protein from rat ventral prostate was studied by light and electron microscopic immunocytochemistry. An anti-22 kDa protein antiserum was raised in rabbits and its specificity was tested by Western blotting. With the immunofluorescence technique, the 22 kDa protein was detected in the luminal secretions and intracellular apical granules of the ventral prostate. No reaction was observed in the seminal vesicle or dorsolateral prostate. After castration, no intracellular immunoreactivity was detected in ventral prostate, although positively labeled secretory material was retained within the acinar lumen. Restoration of normal intracellular staining pattern was incomplete after 5 daily testosterone injections. At the ultrastructural level, labeling was confined to apical secretory granules and condensing vacuoles. The 22 kDa protein separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred to nitrocellulose was shown to bind intensely to wheat germ agglutinin (WGA) but only faintly to Concanavalin A. This protein was thus demonstrated to contain N-acetylglucosamine residues. Accordingly, on tissue sections, WGA reacted intensely with condensing vacuoles and secretory granules.

Animals↗