Molecular cloning of cDNAs for mouse low-molecular-weight and high-molecular-weight prekininogens

Takano, Masaoki; Kondo, Junya; Yayama, Katsutoshi; Otani, Mieko; Sano, Keiji; Okamoto, Hiroshi

doi:10.1016/s0167-4781(97)00018-3

Cited by 31 publications

(33 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Elevations of Lkininogen mRNA levels were observed 7, 14 and 28 d after aortic constriction. Increased levels of tissue kallikrein mRNA were also present at 14 and 28 d. In agreement with our previous findings, 24) no signals corresponding to Hkininogen mRNA were detected in either sham-operated or experimental animals with aortic constriction. DISCUSSION ACE inhibitors are highly effective in the treatment of cardiac hypertrophy within the context of cardiac remodeling.…”

Section: Cardiac Hypertrophy After Aortic Constrictionsupporting

confidence: 92%

“…24) The probe for mouse tissue kallikrein was an oligonucleotide with a sequence of 5Ј-GGTTGTGGGGTCTGCTCATTCAGGA-3Ј that corresponded to nucleotides 343-368 of mK1 mRNA, 25) and the B2 receptor was a 417 bp fragment of mouse B2 receptor cDNA obtained by PCR amplification using RNA from mouse heart as a template following TA cloning. 26) Although samples from sixty-nine mice were analyzed, data in figures show representative blots from two aortic-constricted and two sham-operated animals per day.…”

Section: Methodsmentioning

confidence: 99%

“…Like humans, mice express only two types of kininogen mRNAs, such as H-and L-kininogens, from a single kininogen gene 24) and B2 receptor in the heart. 26) For these reasons, we chose in the present study mouse models for the pressureoverload hypertrophy instead of the rat model usually used.…”

Section: Cardiac Hypertrophy After Aortic Constrictionmentioning

confidence: 99%

See 2 more Smart Citations

Expressions of Bradykinin B2-Receptor, Kallikrein and Kininogen mRNAs in the Heart Are Altered in Pressure-Overload Cardiac Hypertrophy in Mice.

Yayama

Hiyoshi

Okamoto

2001

Biological & Pharmaceutical Bulletin

Self Cite

View full text Add to dashboard Cite

Cardiac left ventricular hypertrophy is most commonly associated with hypertension and is an independent risk factor for cardiovascular events in patients with hypertension. Mechanical load or stretching in cardiac tissue has been identified as a growth stimulus and may be relevant in hypertension-induced cardiac hypertrophy.1) Hormonal stimuli, such as angiotensin II, endothelins, norepinephrine, and thyroid hormone, have also been postulated to play a role in the regulation of cardiac cell growh.2-5) Based on the finding that angiotensin II stimulates protein synthesis of cardiac myocytes 6) and that angiotensin-converting enzyme (ACE) inhibitor induces regression of cardiac hypertrophy both in experimental animal models 7) and in hypertensive patients, 8) several studies have suggested a crucial role of the renin-angiotensin system locally present in the cardiac tissue in the formation of hypertrophy. 9) Indeed, the activation of the cardiac renin-angiotensin system, such as the upregulation of angiotensinogen, ACE and angiotensin II type-1 (AT1) receptor mRNAs, have been demonstrated in association with cardiac hypertrophy. [10][11][12][13] In contrast to angiotensin II, kinins produced by the kallikrein-kinin system have been postulated to participate in the beneficial effects of ACE inhibitors, because ACE inhibitors prevent the degradation of kinins into inactive peptides by inhibiting kininase II, and B2 receptor antagonist abolished the reduction of cardiac hypertrophy by an ACE inhibitor in the rat aortic-banding model. 14,15) Kinins are released from high-and low-molecular-weight kininogens (H-and L-kininogens, respectively) by kininogenases such as plasma and tissue kallikreins.16) Evidence suggests that a local kallikrein-kinin system exists in the heart, which enables it to synthesize and release kinins. 17) In this respect, we have demonstrated that rat cardiac myocytes express mRNAs for bradykinin B2-receptor, kininogen and kallikrein, supporting the presence of the local kallikreinkinin system in the heart. 18) Recent studies have provided evidence that kinins released locally in the heart may act as autocrine/paracrine hormones, inhibiting the cardiac remodeling process, such as cardiomyocyte hypertrophy and hyperplasia of interstitial fibroblasts, suggesting that kinins are cardioprotective factors inhibiting the progression of cardiac hypertrophy. [19][20][21][22] In these studies, however, alterations of the cardiac kallikrein-kinin system during the formation of hypertrophy were not investigated. We hypothesized that the cardiac kallikrein-kinin system may be altered during the development of heart failure and may contribute to the pathophysiology of this disease state. Therefore, the present study was designed to answer this question by determining mRNA levels of the kallikrein-kinin components, such as kininogens, tissue kallikrein and bradykinin receptors, during the development of pressure-overload cardiac hypertrophy in mice. MATERIALS AND METHODSAbdominal Aorta Constriction Adult male...

show abstract

Section: Cardiac Hypertrophy After Aortic Constrictionsupporting

confidence: 92%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Expressions of Bradykinin B2-Receptor, Kallikrein and Kininogen mRNAs in the Heart Are Altered in Pressure-Overload Cardiac Hypertrophy in Mice.

Yayama

Hiyoshi

Okamoto

2001

Biological & Pharmaceutical Bulletin

Self Cite

View full text Add to dashboard Cite

show abstract

“…3B). Activated PLC cleaves membrane phospholipid PIP2 to produce the two second messengers, IP 3 (Fig. 3B).…”

Section: Plc Inhibitor) Reduced Hk-and Bk (Control)-mediated [Ca 2ϩmentioning

confidence: 99%

“…Therefore, the plasma KKS can be considered to have a spectrum of physiological effects, ranging at one extreme from a hemostatic state of vasodilation and promotion of smooth blood flow, all the way to a prothrombotic state. It is conceivable to suggest that other mechanisms proposed about respiratory, retinal, and renal systems can fit into this spectrum of physiological effects (1)(2)(3). There is accumulating evidence suggesting that when the plasma KKS is activated, the results are a sequential release of proteolytic enzymes and vasoactive peptides, generation of both angiogenic and anti-angiogenic molecules, stabilization of thrombus, and an increase in protease inhibitor activity in blood (4 -7).…”

mentioning

confidence: 99%

High Molecular Weight Kininogen Activates B2 Receptor Signaling Pathway in Human Vascular Endothelial Cells

Kolte

Osman

Yang

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

The nonenzymatic cofactor high molecular weight kininogen (HK) is a precursor of bradykinin (BK). The production of BK from HK by plasma kallikrein has been implicated in the pathogenesis of inflammation and vascular injury. However, the functional role of HK in the absence of prekallikrein (PK), the proenzyme of plasma kallikrein, on vascular endothelial cells is not fully defined. In addition, no clinical abnormality is seen in PKdeficient patients. Therefore, an investigation into the effect of HK, in the absence of PK, on human pulmonary artery endothe- The plasma kallikrein-kinin system (KKS) 2 consists of three proenzymes; factor XII (FXII, Hageman factor), prekallikrein (PK, Fletcher factor), and factor XI (FXI, plasma thromboplastin antecedent) as well as one cofactor; high molecular weight kininogen (HK, Fitzgerald factor). KKS is involved in the regulation of hemodynamics, inflammation, complement activation, angiogenesis, thrombosis, and fibrinolysis. Basically, all these proposed roles represent a range of overlapping effects that contribute to various extents toward vasodilation and healing. Therefore, the plasma KKS can be considered to have a spectrum of physiological effects, ranging at one extreme from a hemostatic state of vasodilation and promotion of smooth blood flow, all the way to a prothrombotic state. It is conceivable to suggest that other mechanisms proposed about respiratory, retinal, and renal systems can fit into this spectrum of physiological effects (1-3). There is accumulating evidence suggesting that when the plasma KKS is activated, the results are a sequential release of proteolytic enzymes and vasoactive peptides, generation of both angiogenic and anti-angiogenic molecules, stabilization of thrombus, and an increase in protease inhibitor activity in blood (4 -7). The activation of HK-PK complex on endothelial cells triggers vasodilation through smooth muscle relaxation, inhibits platelet aggregation, and induces proinflammatory responses. Of note, the direct assembly of HK, PK, and FXII on vascular smooth muscle cells (VSMC) also results in the activation of PK to kallikrein (8). The induction of these physiological reactions is caused by the release of the vasoactive peptide bradykinin (BK) from HK by kallikrein. Bradykinin B 2 receptor activation by BK mediates the activation of endothelial nitric-oxide synthase (eNOS) and phospholipase A 2 (PLA 2 ) leading to production of nitric oxide (NO) and prostacylin (PGI 2 ). Evidence suggests that BK phosphorylates p44/42 mitogen-activated protein kinase in VMSC, which is blocked by BK antagonist HOE-140 (8).Besides having a direct effect on blood vessels, the HK-PK complex has also been shown to mediate the effects of other pro-inflammatory molecules. Recent study suggests that the inhibitors of both BK and factor XII activity protect from mast cell-induced effects not only in patients but also in genetically engineered mouse models. The authors proposed that this class of inhibitors could be useful to treat allergic diseases (9)....

show abstract

Identification and bioactivity evaluation of a novel bradykinin inhibitory peptide from the skin secretion of Chinese large odorous frog,Odorrana livida

Yang

Wang

et al. 2016

J. Pept. Sci.

View full text Add to dashboard Cite

A novel peptide was isolated from the skin secretion of Chinese large odorous frog, Odorrana livida, and was named as Rana-BI. The cDNA sequencing was obtained by 'shotgun' cloning. The amino acid sequence of the mature peptide was identified as Gly-Leu-Leu-Ser-Gly-Lys-Ser-Val-Lys-Gly-Ser-Ile-OH by automated Edman degradation, and the molecular weight of the peptide was confirmed to be 1144.68 Da by MALDI-TOF and liquid chromatography/MS. Subsequently, the bioactivity of synthetic peptide was evaluated by smooth muscle assay using isolated rat bladder preparation. It was demonstrated that Rana-BI inhibited the contraction of rat bladder induced by bradykinin. Comparing with other peptides by searching from database, the primary structure of Rana-BI showed high similarity with that of an antimicrobial peptide of Rana family (12/12 residues). These data revealed a novel biological function of this peptide.

show abstract

Molecular cloning of cDNAs for mouse low-molecular-weight and high-molecular-weight prekininogens

Cited by 31 publications

References 8 publications

Expressions of Bradykinin B2-Receptor, Kallikrein and Kininogen mRNAs in the Heart Are Altered in Pressure-Overload Cardiac Hypertrophy in Mice.

Expressions of Bradykinin B2-Receptor, Kallikrein and Kininogen mRNAs in the Heart Are Altered in Pressure-Overload Cardiac Hypertrophy in Mice.

High Molecular Weight Kininogen Activates B2 Receptor Signaling Pathway in Human Vascular Endothelial Cells

Identification and bioactivity evaluation of a novel bradykinin inhibitory peptide from the skin secretion of Chinese large odorous frog,Odorrana livida

Contact Info

Product

Resources

About