Immunohistochemical localization of rat submandibular gland esterase B (homologous to the RSKG-7 kallikrein gene) in relation to other serine proteases of the kallikrein family.

Berg, Torill; Wassdal, I; Sletten, Knut

doi:10.1177/40.1.1309555

Cited by 23 publications

(11 citation statements)

References 6 publications

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“…The use of two antisera raised in different laboratories stresses the consistency of our findings. The minimal variations produced in the staining after coincubation of the antiserum with rK7, a weak kininogenase [24,25], in the oil-stimulated and unstimulated pseudopregnant horn at Day 7, does not permit us to ascertain the presence or absence of this protein, which should be further studied by mRNA analysis and by in situ hybridization.…”

Section: Discussionmentioning

confidence: 99%

Estrogen and Luminal Stimulation of Rat Uterine Kallikrein1

Corthorn

Figueroa

Valdés

1997

Biology of Reproduction

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To understand the regulation of rat uterine kallikrein, we evaluated its variations in animals that had been ovariectomized and supplemented with estradiol or progesterone, in pseudopregnant animals intraluminally oil-stimulated or unstimulated, and in unilaterally pregnant animals. The content of kallikrein, determined by an RIA highly specific for rK1 (true tissue kallikrein), rose in ovariectomized rats with estradiol supplementation (0.28 +/- 0.03 to 0.44 +/- 0.05 ng/mg) and decreased with progesterone (0.13 +/- 0.02 ng/mg; n = 15; p < 0.001). Kallikrein content rose from Day 1 of pseudopregnancy (PP1) to a maximum on PP7 (0.18 +/- 0.01 to 0.39 +/- 0.04 ng/mg protein; n = 36; p < 0.001). On PP7 with unilateral oil intraluminal stimulation, the decidualized horn had higher kallikrein content than did the contralateral (0.98 +/- 0.09 vs. 0.35 +/- 0.05 ng/mg protein; n = 7; p < 0.001). Immunocytochemistry revealed that mainly rK1 is localized in the luminal and glandular epithelium, and it increased in the stimulated horn. In the unilaterally pregnant rat on Day 7, the fertile horn had a higher kallikrein content than its contralateral control (0.71 +/- 0.07 vs. 0.37 +/- 0.03 ng/mg protein, p < 0.001; n = 8), as well as a higher kininogenase activity (239 +/- 34.3 vs. 83.5 +/- 7.9 ng bradykinin(BK)/h per horn, p < 0.003; and 945 +/- 90 vs. 585 +/- 40 ng BK/h per gram tissue, p < 0.002; n = 6). These results indicate that estrogen stimulates, whereas progesterone inhibits, kallikrein production, and that hormonal regulation is overridden by intraluminal stimulation, thus associating the enzyme with decidualization.

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Section: Discussionmentioning

confidence: 99%

Estrogen and Luminal Stimulation of Rat Uterine Kallikrein1

Corthorn

Figueroa

Valdés

1997

Biology of Reproduction

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“…In addition, some mammal species, including mouse, rat, horse and possibly shrew have elaborated subfamilies of kallikreins specific to them [18], [20], [60]. Previous studies by others identified RNA [23], [61], [62], [63], [64], [65], [66], [67], [68], [69] and protein [70], [71], [72], [73] of kallikrein subfamily genes in rodent submandibular glands. Much of this previous work, however, focused on kallikrein expression in the submandibular glands of males only.…”

Section: Discussionmentioning

confidence: 99%

Positive Selection Shaped the Convergent Evolution of Independently Expanded Kallikrein Subfamilies Expressed in Mouse and Rat Saliva Proteomes

Karn

Laukaitis

2011

PLoS ONE

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We performed proteomics studies of salivas from the genome mouse (C57BL/6 strain) and the genome rat (BN/SsNHsd/Mcwi strain). Our goal was to identify salivary proteins with one or more of three characteristics that may indicate that they have been involved in adaptation: 1) rapid expansion of their gene families; 2) footprints of positive selection; and/or 3) sex-limited expression. The results of our proteomics studies allow direct comparison of the proteins expressed and their levels between the sexes of the two rodent species. Twelve members of the Mus musculus species-specific kallikrein subfamily Klk1b showed sex-limited expression in the mouse saliva proteomes. By contrast, we did not find any of the Rattus norvegicus species-specific kallikrein subfamily Klk1c proteins in male or female genome rat, nor transcripts in their submandibular glands. On the other hand, we detected expression of this family as transcripts in the submandibular glands of both sexes of Sprague-Dawley rats. Using the CODEML program in the PAML package, we demonstrate that the two rodent kallikrein subfamilies have apparently evolved rapidly under the influence of positive selection that continually remodeled the amino acid sites on the same face in the members of the subfamilies. Thus, although their kallikrein subfamily expansions were independent, this evolutionary pattern has occurred in parallel in the two rodent species, suggesting a form of convergent evolution at the molecular level. On the basis of this new data, we suggest that the previous speculative function of the species-specific rodent kallikreins as important solely in wound healing in males be investigated further. In addition to or instead of that function, we propose that their sex-limited expression, coupled with their rapid evolution may be clues to an as-yet-undetermined interaction between the sexes.

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“…It has been shown to induce endothelium-independent aortic contraction through a mechanism other than formation of angiotensin I1 (Berg et al, 1992b;Yamaguchi et al, 1991). Whether this has any physiological significance in the prostate is not known.…”

Section: Discussionmentioning

confidence: 99%

Immunohistochemical localization of rK9, an enzyme of the kallikrein gene family, in the rat ventral prostate.

Berg

Schøyen²

1995

J Histochem Cytochem.

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The rat kallikrein family consists of multiple closely related proteins. Most of these proteins have been purified from rat submandibular gland (SMG), among them rK9, an enzyme that has a direct vasoconstrictory effect on isolated aortic rings. Recently, two members of the kallikrein family, rK8 and rK9, were also purified from rat prostate, whereas other family members were not detected in this organ. In the present study, the immunohistochemical localization of rK9 was determined in rat prostate by the indirect immunofluorescence technique with polyclonal antisera against rat SMG rK9 in the first layer. The crossreactivity pattern of the antiserum against rat prostate tissue extract was established by flat-bed isoelectrofocusing and immunoblotting. The antiserum reacted with prostate rK9 but not with prostate rK8. Specificity of the immunofluorescent staining reaction was verified by staining with the primary antiserum after addition of purified SMG or prostate rK9, or other members of the kallikrein family including prostate rK8. rK9-specific immunofluorescence was detected in the prostate ductal structures. In the distal (acinar) segments, rK9 was found in the cytoplasm as granular staining in the middle third of the cell, in the luminal cell wall, and in the secretion within the lumen. In the intermediate segments, strong rK9-specific staining was observed adhering to the luminal wall as well as abundantly within the ductal lumen.

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Immunohistochemical localization of rat submandibular gland esterase B (homologous to the RSKG-7 kallikrein gene) in relation to other serine proteases of the kallikrein family.

Cited by 23 publications

References 6 publications

Estrogen and Luminal Stimulation of Rat Uterine Kallikrein1

Estrogen and Luminal Stimulation of Rat Uterine Kallikrein1

Positive Selection Shaped the Convergent Evolution of Independently Expanded Kallikrein Subfamilies Expressed in Mouse and Rat Saliva Proteomes

Immunohistochemical localization of rK9, an enzyme of the kallikrein gene family, in the rat ventral prostate.

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