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Results for “Kininogens”

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At least 55 records · Page 3Linked to original sources
PubMed1985

Identification of T-kininogen in high and low molecular weight kininogens deficient rat (brown Norway Katholiek strain).

Kinin release in Brown Norway Katholiek (B/N-Ka) rat plasma was compared with those of Brown Norway Kitasato and Sprague-Dawley rats by treating with rat plasma kallikrein, rat urinary kallikrein, snake venom kininogenase and trypsin. B/N-Ka rat plasma yielded no detectable amount of kinin by either plasma kallikrein, urinary kallikrein or snake venom kininogenase, but yielded variable amount of kinin by trypsin. The released kinin was proved to be isoleucylseryl-bradykinin by high performance liquid chromatography and bioassay profiles. B/N-Ka rat plasma formed a precipitation line against antiserum to T-kininogen, but no line against antiserum to HMW kininogen-light chain.

Animals↗
PubMed1985

Experimental arteriosclerosis and the plasma kininogen and low molecular weight kininogen antigen concentration in rabbits.

A decrease in trypsin-releasable kinin and in low molecular weight kininogen antigen concentrations was observed in plasma of rabbits with cholesterol-induced arteriosclerosis. In rabbits receiving normal diet for 30 days after 30 days of cholesterol almost complete normalization of the morphological status was observed, which was accompanied by normalization of plasma kinin concentration and by higher than normal concentration of kininogen antigen measured. These changes were not observed in animals receiving normal diet for 30 days after 60 days of cholesterol administration. No data were obtained suggesting a massive kinin release during induction of arteriosclerosis by experimental hypercholesteremia. The possibility of intense kinin formation during a period of repair of the morphological changes was discussed.

Animals↗
PubMed1992

Immunolocalization of high molecular weight kininogen (HKg) and T kininogen (TKg) in the rat hypothalamus.

Specific HKg immunostaining detected with antiserum against the light chain (LC) of HKg was restricted to SRIF neurons of the hypothalamic periventricular area projecting to median eminence (ME). Heavy chain (HC) immunoreactivity related to HKg and/or low molecular weight kininogen (LKg) was found in some other hypothalamic territories. Specific TKg was mainly associated with vasopressin in neurons of suprachiasmatic (SCN), supraoptic (SON) and paraventricular (PVN) nuclei. By direct RIA, hypothalamus was found to contain the highest level of TKg (10ng/mg protein) and after trypsin hydrolysis and HPLC separation of kinins, 10.3 pg BK and 7.3 pg T-kinin/mg protein.

Animals↗
PubMed2002

Inhibition of angiogenesis by a monoclonal antibody to kininogen as well as by kininostatin which block proangiogenic high molecular weight kininogen.

High molecular weight kininogen (HK) exhibits two activities with respect to angiogenesis after cleavage by plasma kallikrein. Cleaved HK (HKa) and its cell-binding domain 5 (D5), kininostatin, are potent antiangiogenic polypeptides. They inhibit endothelial cell migration, proliferation and tube formation. HKa and D5 inhibit angiogenesis in the chicken chorioallantoic membrane (CAM) assay. D5 stimulates apoptosis and interferes with the cell cycle. In contrast, intact HK is proangiogenic by liberating bradykinin. A monoclonal antibody to HK can inhibit angiogenesis in the CAM assay, human colon carcinoma growing as a xenograft in nude mice, and murine hybridomas growing in syngeneic hosts. Not only are the tumors decreased in volume and weight to isotype controls but the mean vascular density is decreased. Thus, both D5 and its constituent peptide and monoclonal antibody have potential for inhibiting angiogenesis and tumor growth in human therapy.

Angiogenesis Inhibitors↗
PubMed1994

Demonstration of high-molecular-weight kininogen in kininogen-deficient rat kidneys.

Brown Norway Katholiek (B/N-Ka) is a mutant rat strain deficient in plasma high-molecular-weight (HK) and low-molecular-weight kininogen (LK). It has been reported that the deficiency, caused by defective secretion of HK and LK by the liver, is associated with a point mutation of alanine (163) to threonine in the common heavy chain. In this report we demonstrate by specific radioimmunoassay that the amount of immunoreactive HK antigen in the B/N-Ka kidney was almost the same as that found in the normal Brown Norway rat (Brown Norway Kitasato, B/N-Ki). HK antigen in the kidneys of both strains was immunohistochemically localized at distal tubules with similar intensity in both strains. Among the subcellular fractions of the kidney homogenates, HK antigen was predominantly found in the microsomal fraction of both strains. To see whether this HK antigen is derived from plasma HK or is synthesized in the kidneys, we examined uptake of HK by the tubular cells after incubation with 125I-HK. Only 0.6% of the radioactivity of added 125I-HK was found in the tubular cells of both strains after a 60-min incubation. Messages of HK mRNA from both strains of rats were visualized by PCR at almost the same intensity. These results suggest that HK antigen found in the kidney may be derived mainly from biosynthesis in the kidney itself and partly from uptake of HK from blood. There was no difference in these features of HK between the kidneys of the deficient and the normal B/N rats.

Animals↗
PubMed2002

Inhibition of angiogenesis by two-chain high molecular weight kininogen (HKa) and kininogen-derived polypeptides.

We recently reported that the two-chain form of human high molecular weight kininogen (HKa) inhibits angiogenesis by inducing endothelial cell apoptosis (Zhang et al. 2000). This property appears to be primarily conferred by HKa domain 5 (HKa D5). In this manuscript, we further characterize the activity of these polypeptides toward proliferating endothelial cells, as well as their in vivo anti-angiogenic activity in the chick chorioallantoic membrane (CAM). We also demonstrate that short peptides derived from endothelial cell binding regions in HKa domains 3 and 5 inhibit endothelial cell proliferation and induce endothelial cell apoptosis. Like HKa and HKa D5, peptides derived from the latter domain induce endothelial cell apoptosis in a Zn(2+)-dependent manner, while those derived from domain 3 function independently of Zn2+. The implications of these findings to the regulation of angiogenesis and development of anti-angiogenic therapeutics are discussed.

Angiogenesis Inhibitors↗
PubMed1989

[DNA analysis for the kininogen gene of patients with kininogen deficiency in Japan].

The kininogen (KGN) gene status was examined in 4 families with both high molecular weight (HMW) and low molecular weight (LMW) KGM deficiency and one family with only HMW-KGN deficiency reported in Japan. No abnormal HMW-KGN or LMW-KGN was detected in those with these deficiencies by immunoblot analysis using monoclonal antibodies (HKG-H12, HKG-L7, HKG-L17) for human HMW-KGN. HMW-DNA prepared from peripheral blood leucocytes was digested with endonuclease, EcoRI, Bam HI, Hind III, Sca I, Bg1II, Xba I, Msp I, Pst I, Hpa I, PvuII, HaeIII, Rsa I, Alu I, or Taq I, and studied by Southern blot analysis with human LMW prekininogen cDNA (phKG 36) as a probe. A gross deletion or insertion of the KGN gene was not detected in those with both HMW- and LMW-KGN deficiencies. On the other hand, partial defect in intron 7 (G) was found in those with only HMW-KGN deficiency, suggesting that this defect might be related to abnormality of the alternative RNA splicing events for HMW-prekininogen mRNA.

DNA Probes↗