Kallikreinlike activity in perfusates and urine of isolated rat kidneys

Roblero, J.; Croxatto, H.; García, Raúl; Corthorn, Jenny; Vito, Eduardo L De

doi:10.1152/ajplegacy.1976.231.5.1383

Cited by 74 publications

(21 citation statements)

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“…Alternatively, two or more closely related genes may be expressed in these tissues. The presence of kallikrein mRNA in the kidney at a level equal to that of the pancreas supports the hypothesis (33,34) that the source of urinary kallikrein is synthesis by the kidney. However, because the pancreatic, submaxillary gland, and kidney kallikreins may be identical, it is not possible to exclude a contribution by kidney filtration of circulating pancreatic or submaxillary gland kallikrein into the urine.…”

Section: Identificationsupporting

confidence: 76%

Rat pancreatic kallikrein mRNA: nucleotide sequence and amino acid sequence of the encoded preproenzyme.

Swift¹,

Dagorn²,

Ashley³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

106

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We have cloned via recombinant DNA technology the mRNA sequence for rat pancreatic preprokallikrein. Four cloned overlapping double-stranded cDNAs gave a continuous mRNA sequence of 867 nucleotides beginning within the 5'-noncoding region and extending to the poly(A) tail. The mRNA sequence reveals that pancreatic kallikrein is synthesized as a prezymogen of 265 amino acids, including a proposed secretory prepeptide of 17 amino acids and a proposed activation peptide of 11 amino acids. The activation peptide, although similar in length, is distinct from those of the other classes of pancreatic serine proteases. The amino acid sequence of the predicted active form of the enzyme is closely related to the partial sequences obtained for other kallikrein-like serine proteases including rat submaxillary gland kallikrein, pig pancreatic and submaxillary gland kallikreins, the y subunit of mouse nerve growth factor, and rat tonin. Key amino acid residues thought to be involved in the substrate-cleavage specificity of kallikreins are retained. Hybridization analysis showed relatively high levels of kallikrein mRNA in the rat pancreas, submaxillary and parotid glands, spleen, and kidney, indicating the active synthesis of kallikrein in these tissues.Glandular kallikreins (EC 3.4.21.8) are members of a closely related subfamily of serine proteases that process polypeptide hormone precursors. Other members include the y subunit of nerve growth factor (1), the epidermal growth factor-binding protein (2), and tonin (3). Characteristically, each has a much more limited substrate-cleavage specificity than other serine proteases such as trypsin, chymotrypsin, and elastase. These kallikrein-like proteases cleave at one or a very few peptide bonds in their natural substrates with a general, but not absolute, preference for residues that have positively charged side chains and a strong bias for arginine over lysine (4,5 4).Kallikreins are found in many exocrine tissues, although their site(s) of synthesis remains unverified, and the nature and processing of presumed kallikrein precursors are unknown. Inactive precursor forms of kallikrein have been purified from rat (6) and porcine (7) pancreas. The precursors are acidic glycoproteins of apparent Mr 37,000. Slow activation occurs spontaneously and is accelerated by catalytic amounts oftrypsin. The activated enzymes are single polypeptides with slightly reduced molecular weight, suggesting the release of an activation peptide, which remains uncharacterized. Active kallikrein isolated from autolysed porcine pancreas consists of two polypeptide chains held together by disulfide bridges (8), indicative of further proteolysis.We report the identification and sequence analysis of the cloned mRNA sequence for rat pancreatic kallikrein and describe the nature of the preproenzyme and the presence of kallikrein mRNA in a number of rat tissues.

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Section: Identificationsupporting

confidence: 76%

Rat pancreatic kallikrein mRNA: nucleotide sequence and amino acid sequence of the encoded preproenzyme.

Swift¹,

Dagorn²,

Ashley³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

106

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“…In rats, however, aldosterone modulated in vivo Na+,K+-ATPase activity in all renal tubular structures studied (39). If kallikrein and prekallikrein were also located on the basal membrane of the epithelial cells of the distal tubules, the role of kallikrein in renal vascular resistance (40,41) and its release into circulation (32) and extracellular fluid (33) …”

Section: Discussionmentioning

confidence: 99%

Activation of membrane-bound kallikrein and renin in the kidney.

Nishimura¹,

Alhenc-Gelas²,

White³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

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Rat kidney contains membrane-bound renin (EC 3.4.99.19) and kallikrein (EC 3.4.21.8). Kallikrein activity was measured by a spectrophotometric assay and renin by radioimmunoassay. Plasma membrane-bound kallikrein was activated by lysolecithin and by melittin, which was a more potent activator. This activation by mellitin was independent of calcium concentration. Melittin was, however, a more potent activator of membrane-bound renin in the presence of calcium. Administration of aldosterone to rats for 6 days increased kallikrein activity in the renal homogenate and in the membraneenriched fractions, whereas renin activity was not affected. It was proposed that kallikrein may also be located on the basal membrane of tubular epithelial cells, where aldosterone can enhance its activity.

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“…Roblero et al 36 ) have observed the urinary excretion of kallikrein in an experiment using isolated rat kidneys perfused with fluid devoid of prekallikrein and kallikrein, and concluded that urinary kallikrein was derived from the kidney. It has also been reported that renal kallikrein was related to the regulation of renal circulation and sodium metabolism via the production of kinin.…”

Section: Discussionmentioning

confidence: 99%