Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Antibodies raised against porcine pancreatic phospholipase A2 (PLA2) react in immunoblottings with both the antigen as well as with one protein band of about 14 kDa from hamster spermatozoa extracts. Immunoblottings of proteins extracted from spermatozoon head and tail fractions also show similar results. Anti-PLA2 purified IgGs were employed for light and electron microscopic immunocytochemistry in order to detect PLA2 in hamster cauda epididymal spermatozoa. When whole mount spread spermatozoa were used under light (employing the PAP complex) or electron microscopy (using anti-rabbit gold conjugated), the acrosomal area of the gametes shows a noticeable labelling; a characteristic which is not observed in samples treated with the pre-immune serum. Immunocytochemistry undertaken in ultrathin sections from spermatozoon samples embedded in Lowicryl, demonstrates that the antigen appears preferentially distributed in the acrosome. Besides, sperm tails showed a scattered distribution of gold granules in the mitochondria of the midpiece. Results suggest that the antibody used recognizes a PLA2 which is preferentially located in the acrosome and mitochondria. On the other hand, the presence of a surface PLA2 in the plasma membrane covering the acrosome is suggested. This surface PLA2 would be probably related to the acrosome reaction phenomenon that occurs in the spermatozoon before penetrating the oocyte.
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PMID:Immunocytochemical localization of phospholipase A2 in hamster spermatozoa. 161 36

In 56 males, vasectomized 8 years previously, and in 56 age-matched non-vasectomized controls, a number of secretory products of prostatic, seminal vesicular and epididymal/testicular origin were used to monitor post-operative changes in accessory sex gland function. Significant reductions were observed in seminal plasma volume (3.0 vs 4.9 ml, P less than 0.01), and the total ejaculate contents of zinc (5.1 vs 9.7 mumol, P less than 0.01), magnesium (10.6 vs 26.5 mumol, P less than 0.01), PAP (371 vs 1260 IU, P less than 0.005) and citric acid (76.7 vs 127.9 mumol, P less than 0.05), indicating a major impact on secretions of prostatic origin. Unaltered PGE-1 (54.3 vs 53.2 micrograms, P less than 0.95) and fructose (3.9 vs 4.5 mumol, P greater than 0.1) indicated no effects on the secretory function of the seminal vesicles. A marked reduction was demonstrated in the ejaculatory contents of the polyamines, spermidine (366 vs 650 nmol, P less than 0.005) and spermine (5435 vs 11 804 nmol, P less than 0.05) but not their acknowledged precursor, putrescine, which is also of prostatic origin.
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PMID:Polyamines and other accessory sex gland secretions in human seminal plasma 8 years after vasectomy. 262 11

Excessive fatty acid release from the white adipose tissue (WAT) contributes to the development of alcoholic liver disease (ALD). Lipin1 (LPIN1), as a co-regulator of DNA-bound transcription factors and a phosphatidic acid (PA) phosphatase (PAP) enzyme that dephosphorylates PA to form diacylglycerol (DAG), is dramatically reduced by alcohol in the WAT. This study aimed at determining the role of adipose LPIN1 in alcohol-induced lipodystrophy and the development of ALD. Transgenic mice overexpressing LPIN1 in adipose tissue (LPIN1-Tg) and wild type (WT) mice were fed a Lieber-DeCarli alcohol or isocaloric maltose dextrin control liquid diet for 8 weeks. Alcohol feeding to WT mice resulted in significant liver damage, which was significantly alleviated in the LPIN1-Tg mice. Alcohol feeding significantly reduced epididymal WAT (EWAT) mass, inhibited lipogenesis, and increased lipolysis in WT mice, which were attenuated in the LPIN1-Tg mice. LPIN1 overexpression also partially reversed alcohol-reduced plasma leptin levels. In WT mice, alcohol feeding induced hepatic lipid accumulation and down-regulation of beta-oxidation genes, which were dramatically alleviated in the LPIN1-Tg mice. LPIN1 overexpression also significantly attenuated alcohol-induced hepatic ER stress. These results suggest that overexpression of LPIN1 in adipose tissue restores WAT lipid storage function and secretive function to alleviate alcohol-induced liver injury.
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PMID:Adipose-specific lipin1 overexpression in mice protects against alcohol-induced liver injury. 2932 42