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Biomedical subjects

S Nagase

Publications and source records attributed to S Nagase.

At least 217 records · Page 12Linked to original sources
PubMed1982

Linkage of the analbuminemia locus (alb) and the hooded locus in the rat, Rattus norvegicus.

A linkage study of the analbuminemia (alb) with some coat color loci (a,b,c,h) has been carried out by crossing the analbuminemic random-bred mutant NAR strain with the abh tester strain of rats, the Agouti-Irish inbred ACI strain and the Agouti-Nonhooded inbred IS strain. The analbuminemia (alb) locus is not linked to a, b, and c loci but linked to hooded locus from F2 and backcross progeny of the F1 hybrids of abh X NAR, ACI X NAR and IS X NAR to NAR. Recombination value between alb and h was 16.4 +/- 2.3 per cent from the data of F2 and backcross progeny of (ACI X NAR) F1 and (IS X NAR) F1 to NAR. This is the third locus on the sixth linkage group of the rat.

Animals↗
PubMed1981

Establishment of an albumin-deficient and jaundiced strain of rats.

An albumin deficient and jaundiced rat (AJR) strain was established from crosses between Albumin-Deficient rats (NAR) and jaundiced Gunn rats. AJRs have a double homozygous mutant trait (alb/alb, j/j), and systemic jaundice and various neurological signs are observed 5--7 days after birth, kernicterus occurs and they die within three weeks after birth. This strain of rats may serve as a model of human kernicterus and also be useful in elucidating the mechanism of bilirubin metabolism.

Animals↗
PubMed1981

[Clinico-biochemical study on Ishibashi rats (author's transl)].

Ishibashi rats, a mutant strain with congenital spinal malformation discovered by Ishibashi in 1968, are generally regarded as an animal model for a human inborn error of spinal malformation. Biochemical values in serum or plasma of Ishibashi rats were compared with those of Wistar-Imamichi rats, and the following results were obtained: 1) In Ishibashi rat sera, alkaline phosphatase activity was significantly lower than that in sera of controls, and an intestinal type of isozyme was hardly detected. 2) All other serum biochemical parameters examined showed no significant difference between Ishibashi and Wistar-Imamichi rats. 3) The data suggest that Ishibashi rats may serve as an animal model of hypophosphatasia in man.

Alkaline Phosphatase↗
PubMed1981

Changes of amylase during experimental pancreatic carcinogenesis in hamsters.

Changes of amylase activity and isozymic pattern in the serum, urine, ascites, pancreas and parotid gland of hamsters during pancreatic carcinogenesis induced by N-nitrosobis (2-oxopropyl) amine (BOP) were examined. During the early stage of pancreatic carcinogenesis, amylase activity in the urine was greatly increased and the pancreatic type of isozyme increased in the serum and urine, but in the terminal stage, the activity decreased and the isozymic pattern reverted to normal. These alterations of amylase could be due to focal pancreatitis around dysplastic ductules and small carcinoma lesions causing leakage of pancreatic juice. This phenomenon may be of value in diagnosis of the early stage of pancreatic cancer.

Adenocarcinoma↗
PubMed1980

Absence of albumin mRNA in the liver of analbuminemic rats.

Albumin synthesis in the liver of analbuminemic rats, established as a strain from a stock of Sprague-Dawley rats, was examined in vivo by labeling protein by intraperitoneal injection of L-[3H]leucine. Albumin was not synthesized in the liver of analbuminemic rats, whereas its synthesis amounted to about 14% of the total protein synthesis in the liver of normal rats. The RNA content and size distribution of the total polysomes in the liver of analbuminemic rats were not significantly different from those of normal rats. However, no functional mRNA coding for albumin was found in poly(A)-containing RNA from the liver of analbuminemic rats when tested with a cell-free translation system derived from rabbit reticulocytes. Moreover, the amount of the RNA sequence that could hybridize to purified albumin cDNA was more than 750 times greater in the liver of normal rats than in that of analbuminemic rats.

Animals↗
PubMed1980

Characterization of hyperlipidemia in Nagase analbuminemia rat (NAR).

The mutant analbuminemia rat (NAR) was recently reported by Nagase (1) to spontaneously develop hypercholesterolemia. A detailed lipid analysis was carried out to characterize the hyperlipidemia. The concentrations of major phospholipids as well as cholesterol were increased in plasma, whereas the triacylglycerol level remained unchanged. Free fatty acid and lysophosphatidylcholine levels, on the contrary, declined. The liver lipids were not accumulated, but appeared to be depleted.

Animals↗
PubMed1980

Absence of albumin in tissues of analbuminemic rats.

Nagase analbuminemic rats (NAR) are deficient in serum albumin. Extravascular regions of the tissues of NAR were tested for rat serum albumin by the immunofluorescence staining technique. Albumin was not detectable in any of the tissues of NAR tested (liver, kidney, muscle, skin, and small intestine), whereas it was clearly demonstrated in all these tissues of normal rats. Furthermore, extracts of NAR tissues, including the liver, contained no albumin detectable by the single radial immunodiffusion method. These findings indicate that albumin is not present in either the serum or extravascular regions of tissues of NAR, and suggest that the deficiency of serum albumin in NAR is not due to impaired albumin secretion from the liver or alteration of the tissue distribution of albumin in certain tissues, but to the absence of its synthesis in the liver.

Albumins↗
PubMed1980

Isolation and characterization of proteodermatansulfate from rat skin.

A proteodermatansulfate was extracted from rat skin with 4 M guanidine hydrochloride containing protease inhibitors at 4 degrees C. It was separated from collagen on DEAE-cellulose in 7 M urea and was purified by cesium chloride density gradient centrifugation under associative conditions, DEAE-Sephadex column chromatography and then Sephadex G-200 gel filtration. On SDS-disc electrophoresis, the proteoglycan gave a single band staining for protein and a band of the same mobility staining with periodate-Schiff reagent. The proteoglycan contained 46% protein, and this was bound to dermatansulfate via an O-glycosidic linkage. The proteoglycan also contained 20% uronic acid and 16% hexosamine, but no detectable hydroxyproline. The ratio of galactosamine to glucosamine was 68. The dermatansulfate, the only glycosaminoglycan, had a hybrid structure containing iduronic acid and glucuronic acid as uronic acids. The content of glucuronic acid in uronic acid was much higher than that of pig skin dermatansulfate. The dermatansulfate had a slightly higher mobility on cellulose acetate electrophoresis than those from other sources. Gel chromatography on Sepharose CL-6B showed that the molecular weight of the dermatansulfate was 23,000, while that of the proteoglycan was 36,000. The elution profile of a mixture of the proteoglycan and hyaluronic acid on Sepharose 6B column chromatography was similar to that of the proteoglycan alone.

Animals↗
PubMed1980

Albumin-deficient rat mutant: an animal model for analbuminemia.

An analbuminemic rat colony (NAR, Nagase Analbuminemia Rat) was established from Sprague-Dawley rats. The Analbuminemia was inherited as an autosomal recessive trait. The rate of growth or propagation of the mutant rats was not different from those of normal rats. Biochemically the mutant was characterized by an extraordinarily low serum albumin and hyperlipidemia. Total protein level of the serum in the mutant rat was similar to that of control Sprague-Dawley rats and globulin increased compensatorily. Serum cholesterol concentration was inversely correlated with a decrease in albumin, its correlation coefficient was -0.92. NAR may serve as a model of human familial analbuminemia. It should be also useful in elucidating the functional roles of albumin.

Animals↗
PubMed1979

Albumin-deficient rat mutant.

An analbuminemic colony was established from Sprague-Dawley rats. Analbuminemia was inherited as an autosomal recessive trait. The rates of growth and reproduction of the mutant rats were no different from those of normal rats. Biochemically, the mutant was characterized by an extraordinarily low serum albumin content and a hyperlipidemia. Total serum protein in the mutant rat was similar to that of control Sprague-Dawley rats, with increased globulin. Serum cholesterol was inversely correlated with a decrease in albumin; the correlation coefficient for ablumin was --.92. These mutant rats may serve as a model of human familial analbuminemia and may also be useful in elucidating the functional roles of albumin.

Animals↗
PubMed1979

[Comparative studies on release of enzymes from platelets during blood clotting in Rattus rattus flavitecus and Rattus norvegicus (author's transl)].

Increase of lactate dehydrogenase (EC 1.1.1.28) and creatine kinase (EC 2.7.3.2) in serum and plasma level during blood clotting was compared in R. rattus flavitectus (black rat) and R. norvegicus (albino rat). Both the enzyme level increased by the release from platelets in process of clotting in rat as previously described (Emori T., Takahashi M. and Nagase S. (1978) Exp. Animals, 27, 167), but the change in black rat was very slight. Owing to search for the reason to prove the difference in this phenomenon, physiological and chemical properties of blood from both the animals were compared, and it was demonstrated that the content of plasma fibrinogen in black rat is higher than that in albino rat, while the platelet number contained in each ml of blood and the enzyme activities in each platelet are not different between them. The analysis of the membrane proteins from platelets of both the animals by SDS-polyacrylamide gel electrophoresis showed that the fractional value of glycoproteins was found to be different between them.

Animals↗