High impact information on SPAM1

• Bovine testicular hyaluronidase PH-20 activates JNK1 and protects L929 fibroblasts from staurosporine-mediated cell death [1].
• In AtT-20 cell lines transfected with a complementary DNA (cDNA) encoding the full-length bPAM precursor, both SPAM and PAM activities were increased compared to wild type cells; both activities were decreased in a cell line expressing an antisense rat (r)PAM mRNA [2].
• Like PAM, SPAM activity is localized to the secretory granule [2].
• The soluble hyaluronidase from bull testes is a fragment of the membrane-bound PH-20 enzyme [3].
• Characterization of PH-20 in canine spermatozoa and testis [4].

Biological context of SPAM1

• The core nucleotide sequence of bovine (Bos taurus) testicular PH-20 hyaluronidase was cloned using one step RT-PCR [5].

Anatomical context of SPAM1

• In marked contrast, an AtT-20 cell line transfected with a cDNA encoding a truncated, soluble form of bPAM had elevated levels of PAM activity, but levels of SPAM activity were not increased compared to wild-type cells [2].
• This study provides evidence that PH-20 is present on the membrane of canine spermatozoa and in round spermatids [4].
• For immunolabeling of PH-20 on canine sperm membranes, canine sperm were fixed and incubated with R-10 primary antibody, and an anti-rabbit IgG-FITC secondary antibody [4].

Associations of SPAM1 with chemical compounds

• Our results thus show that the soluble 60-kDa hyaluronidase from bovine testes is a glycoprotein derived from the sperm PH-20 enzyme [3].
• The hyaluronidase activity of canine PH-20 was determined with substrate gel electrophoresis based upon digestion of hyaluronic acid (HA) incorporated into the separating gels [4].
• Canine spermatozoa were extracted with Triton X- 100 and the presence of PH-20 was determined by immunoblot with an antibody against recombinant macaque PH-20 [4].

Analytical, diagnostic and therapeutic context of SPAM1

• In rat anterior pituitary this factor (denoted SPAM for stimulator of PAM activity) was a soluble protein with a mol wt of 44 K by gel filtration; its stimulatory activity could be reduced or eliminated by trypsin digestion or boiling [2].

References