A 33-kD glycoprotein, known as the "prostate-specific antigen," was purified to homogeneity from human seminal plasma. The prostatic protein was identified as a serine protease, and its NH2-terminal sequence strongly suggests that it belongs to the family of glandular kallikreins. The structural protein of human seminal coagulum, the predominant protein in seminal vesicle secretion, was rapidly cleaved by the prostatic enzyme, which suggests that this seminal vesicle protein may serve as the physiological substrate for the protease. The prostatic enzyme hydrolyzed arginine- and lysine-containing substrates with a distinct preference for the former. All synthetic substrates tested were poor substrates for the enzyme. Synthetic Factor XIa substrate (pyro-glutamyl-prolyl-arginine-p-nitroanilide), and the synthetic kallikrein substrate (H-D-prolyl-phenylalanyl-arginine-p-nitroanilide) were hydrolyzed with maximum specific activities at 23 degrees C of 79 and 34 nmol/min per mg and Km values of 1.0 and 0.45 mM, respectively. Synthetic substrates for plasmin, chymotrypsin, and elastase were either not hydrolyzed by the enzyme at all, or only hydrolyzed very slowly.

/pdf/a-kallikrein-like-serine-protease-in-prostatic-fluid-cleaves-4xkuhbhwun.pdf

A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein.

Since the discovery of kallikreins in the submandibular glands in 1963 by Werle and Roden, a great number of biologically active polypeptides has been purified from, or claimed to be present in, the submandibular of the mouse and of other species In this review, available data on the occurrence, chemical properties, localization, hormonal control, synthesis, secretion, and possible physiologic roles of 25 biologically active factors in mouse submandibular gland are analyzed In general, these factors are androgen dependent, but not affected by the sex genotype, and are localized in the granular convoluted tubule cells in the gland They are secreted into the saliva, but are also found in the circulation Their physiologic roles are largely unknown

Biologically active polypeptides in submandibular glands.

Snake venom proteases affecting hemostasis and thrombosis.

The glandular kallikrein gene family comprises 25–30 highly homologous genes that encode specific proteases involved in the processing of biologically active peptides. In the mouse all the members of this family are closely linked on chromosome 7. The 9.5-kilobase nucleotide sequence of a mouse genomic clone contains one complete kallikrein gene (mGK-1), which is expressed in the male mouse submaxillary gland, and the 3′ end of another (mGK-2). Differences in the coding potential of these genes and the amino acid sequences of other known kallikreins seem to be functionally related to the substrate specificity of the different enzymes.

Structure of mouse kallikrein gene family suggests a role in specific processing of biologically active peptides.

The 15 members of the kallikrein-related serine peptidase (KLK) family have diverse tissue-specific expression profiles and putative proteolytic functions. The kallikrein family is also emerging as a rich source of disease biomarkers with KLK3, commonly known as prostate-specific antigen, being the current serum biomarker for prostate cancer. The kallikrein locus is also notable because it is extraordinarily responsive to steroids and other hormones. Indeed, at least 14 functional hormone response elements have been identified in the kallikrein locus. A more comprehensive understanding of the transcriptional regulation of kallikreins may help the field make more informed hypotheses about the physiological functions of kallikreins and their effectiveness as biomarkers. In this review, we describe the organization of the kallikrein locus and the structure of kallikrein genes and proteins. We also focus on the transcriptional regulation of kallikreins by androgens, progestins, glucocorticoids, mineralocorticoids, estrogens, and other hormones in animal models and human prostate, breast, and reproductive tract tissues. The interaction of the androgen receptor with androgen response elements in the promoter and enhancer of KLK2 and KLK3 is also summarized in detail. There is evidence that all kallikreins are regulated by multiple nuclear receptors. Yet, apart from KLK2 and KLK3, it is not clear whether all kallikreins are direct transcriptional targets. Therefore, we argue that gaining more detailed information about the mechanisms that regulate kallikrein expression should be a priority of future studies and that the kallikreinlocuswillcontinuetobeanimportantmodelintheeraofgenome-wideanalyses.(EndocrineReviews 31: 407–446, 2010)

/pdf/kallikreins-on-steroids-structure-function-and-hormonal-1njud0ijm4.pdf

Kallikreins on steroids: structure, function, and hormonal regulation of prostate-specific antigen and the extended kallikrein locus.

Guinea-pig submandibular kallikrein has been purified from the glands to electrophoretic homogeneity by conventional procedures. The enzyme is active as a kininogenase, releasing kallidin at a rate of 462 micrograms/min per mg of protein from bovine kininogen, and proved potently hypotensive in the guinea pig and in the dog, properties which indicate its tissue kallikrein nature. The specific activity determined on the substrate N-alpha-benzoyl-L-arginine ethyl ester (11.1 mumol/min per mg of protein) is much lower than that measured with N-acetyl-L-phenylalanyl-L-arginine ethyl ester (483 mumol/min per mg of protein). The latter value is of an order of magnitude comparable with the specific activities of other tissue kallikreins determined with this sensitive kallikrein substrate. The enzyme is a glycoprotein consisting of 237 amino acid residues and containing three to four glucosamine molecules. Its amino acid composition is not identical with that reported for guinea-pig coagulating-gland kallikrein, but is remarkably similar to that of the porcine tissue kallikreins. Apparent Mr values are 29000 (sodium dodecyl sulphate/polyacrylamide-gel electrophoresis) or 34000 (gel filtration). The amino acid sequence of the first 31 N-terminal residues was determined and was found to be closely homologous with that of other tissue kallikreins.

/pdf/purification-and-properties-of-guinea-pig-submandibular-vgnohh5pcc.pdf

Purification and properties of guinea-pig submandibular-gland kallikrein.

The relatively early interest in pancreatic kallikrein has led to the ready availability of this enzyme in a pure form. As a result, much more is known of the chemistry of pancreatic kallikrein (for example, see Kutzbach & Schmidt-Kastner, 1973) than of submaxillary or urinary kallikrein.

Isolation of porcine submaxillary kallikrein.

The amino acid sequence of the A- and B-chains of porcine pancreatic kallikrein B is presented and compared to that of porcine trypsin. The overall homology between both enzymes is 37% identical residues in corresponding position and 51% chemically similar residues. Comparison of the sequences with the crystal structure of bovine trypsin reveals that the trypsin “autolysis loop” is enlarged in kallikrein by two residues but lacks the basic residue at the cleavage site. Substitutions at the calcium-binding site of trypsin which include Arg 70 for Glu 70 possibly interfere with ion binding. Insertions between trypsin residues 95 and 96 obviously form a new kallikrein “autolysis loop” containing the site of cleavage between the A- and B-chains. One carbohydrate moiety is attached to this surface loop at Asn 95, the second to Asn 239 at the same edge of the globular molecule. The residues at the surface of the substrate binding site are substituted to an extent of 85% while the residues forming contacts to the trypsin inhibitor (Kunitz) are highly preserved. Immunodiffusion studies as well as identity of the N-terminal sequences of pancreatic, submandibular and urinary kallikrein reveal the same genetic origin of the three glandular kallikreins.

The Primary Structure of Porcine Glandular Kallikreins

The kallikrein from pig submandibular glands was highly purified, with an overall yield of 31%. Affinity chromatography on bovine basic pancreatic trypsin inhibitor linked to Sepharose 4B was an especially effective step in the purification procedure, giving a purification factor of 80. The enzyme is a single-chain molecule, occurring, as does pig urinary kallikrein, as a major B-form of apparent mol.wt. 39600 and minor amounts of an A-form of apparent mol.wt. 35900; the two forms can be separated by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The amino acid composition of pig submandibular kallikrein is very similar to, but not quite identical with, that of the two-chain β-kallikrein isolated from pig pancreatic autolysates. Submandibular kallikrein contains notably more glucosamine and hexoses than does pancreatic β-kallikrein. Submandibular kallikrein, and also urinary kallikrein, exhibit an unusual biphasic hydrolysis of substrate esters that is not shared by pancreatic β-kallikrein. For the submandibular enzyme, the Km for the initial reaction phase of the hydrolysis of α-N-benzoyl-l-arginine ethyl ester is 0.15±0.01mm (mean±s.e.m.), but rises to 0.69±0.04mm (mean±s.e.m.) in the stationary reaction phase; the Vmax. does not differ significantly between the two phases. The esterolytic activities of submandibular and urinary kallikreins on a number of esters of different amino acids resemble each other much more closely than those of pancreatic β-kallikrein.

/pdf/the-isolation-and-properties-of-pig-submandibular-kallikrein-5014fa4srr.pdf

The isolation and properties of pig submandibular kallikrein

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Purification and properties of guinea-pig submandibular-gland kallikrein.

Isolation of porcine submaxillary kallikrein.

The Primary Structure of Porcine Glandular Kallikreins

The isolation and properties of pig submandibular kallikrein