Gastricsin in the benign and malignant prostate.

Reid, William A.; Liddle, C N; Svasti, Jisnuson; Kay, John

doi:10.1136/jcp.38.6.639

Cited by 13 publications

(1 citation statement)

References 8 publications

(1 reference statement)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Reid et al (1985) have demonstrated the production of PGC by the benign prostate. However, Sanchez et al (1992) determined the active role of PGC in the breast tumor progression and showed that PGC may play a direct role in the development of such diseases.…”

Section: Pgc As a Biomarkermentioning

confidence: 99%

Progastriscin: Structure, Function, and Its Role in Tumor Progression

Hassan

Toor

Ahmad

2010

Journal of Molecular Cell Biology

View full text Add to dashboard Cite

Progastricsin (PGC) is a major seminal plasma protein having aspartyl proteinases-like activity and showing close sequence similarity to pepsins. PGC is also present as zymogen in gastric mucosa. In this article, we have reviewed all important features of PGC. Furthermore, we have compared all features of PGC with those of different aspartyl proteinases. The complete amino acid sequence of PGC reveals that it is composed of 374 residues (gastricsin moiety of 331 residues and the activation segment of 43 residues). The gene of human PGC is located at single locus on chromosome 6, whereas the human pepsinogen genetic locus is polymorphic and codes for at least three distinct polypeptide sequences on chromosome 11. The major useful function of PGC includes production of pro-antimicrobial substance in seminal plasma. The crystal structure of human PGC is known, which shows that it is quite similar to that of porcine pepsinogen. The tertiary structure of PGC is comprised of commonly bilobal structure with a large active-site cleft between the lobes. Two aspartate residues in the center of the cleft, namely Asp32 and Asp215, function as catalytic residues. The sequence and structural features of PGC indicate that it is diverged from its pepsinogen ancestor in the early phase of the evolution of gastric aspartyl proteinases. Our detailed review of PGC structure, function and activation mechanism will also be of interest to cancer biologists as well as gastroenterologists.

show abstract

Section: Pgc As a Biomarkermentioning

confidence: 99%

Progastriscin: Structure, Function, and Its Role in Tumor Progression

Hassan

Toor

Ahmad

2010

Journal of Molecular Cell Biology

View full text Add to dashboard Cite

show abstract

Identification of primary tumour site by immunolocalization of progastricsin in metastatic adenocarcinoma

Reid

Branch

Gorman

et al. 1990

The Journal of Pathology

View full text Add to dashboard Cite

The aspartic proteinase zymogen, progastricsin, which occurs in normal gastroduodenal mucosa and prostate, has been localized by the immunogold-silver method in formalin-fixed, paraffin-embedded sections of metastatic adenocarcinoma in lymph nodes and liver, the primary site being known in each case. Progastricsin was demonstrated in 16 of 84 lymph node metastases, including 7 of 17 from stomach, 2 of 2 from prostate, and 7 of 65 from other sites. Progastricsin was also found in 19 of 98 hepatic metastases, including 8 of 22 from stomach, 6 of 24 from pancreas, and 5 of 52 from other sites. The presence of progastricsin in a metastasis correlated well with a primary tumour in the stomach or prostate or, less significantly, pancreas. Immunolocalization of progastricsin in a histological section of metastatic adenocarcinoma may help to locate the primary site.

show abstract