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T Komoda

Publications and source records attributed to T Komoda.

At least 109 records · Page 6Linked to original sources
PubMed1989

Relationship between the uptake of calcium or phosphorus and alkaline phosphatase activity induced by certain modulators in rat organs.

The effects of phorbol ester or calmodulin on the calcium and phosphorus uptakes by rat tissues and their relationship to the alkaline phosphatase activity (ALP) were investigated in vivo. In rat tissues, ALP activity and calcium uptake in the duodenum and liver were clearly induced by phorbol ester treatment, whereas in the calvarium and ileum they were decreased. Phosphorus uptake was increased by the administration of phorbol ester only in the calvarium. In rats pretreated with an injection of indomethacin as an inhibitor of prostaglandin-synthesizing enzyme, the selective uptake of calcium by phorbol ester was eliminated in the duodenum and liver, as was the ALP activity. In contrast, rats showed a marked increase in ALP activity in the ileum after calmodulin treatment. Moreover, the increased uptake of calcium after calmodulin treatment was clearly seen in the ileum, calvarium, and kidney, and an increased uptake in phosphorus was seen in the duodenum, ileum, and calvarium, but not in kidney. Furthermore, prior injection of W-7 or calmidazolium as an antagonist of calmodulin, reduced the increased ALP activities and the uptake of calcium in all organs tested, but did not reduce the increased phosphorus uptake by the calvarium. Consequently, it is suggested that calcium uptake under the above conditions correlated well with changes in the ALP activity; however, phosphorus uptake seemed to be less in accord with ALP activity. The amount of tested other mineral metabolic markers suggests that the Ca uptake and ALP activity induced by certain effectors regulate 1,25(OH)2D3 level by the modulation of 25(OH)D3-1 alpha-hydroxylase activity.

Alkaline Phosphatase↗
PubMed1989

[CA 19-9 like epitope(s) on carcinoembryonic antigen molecules].

CA 19-9 epitope(s) on carcinoembryonic antigen (CEA) was studied by a method designated the hybrid immunoradiometric-assay (hybrid IRMA) using solid phase CEA antibody to capture the CEA molecule and radio-labeled NS 19-9 antibody as a detector. The radioactivities of the hybrid IRMA of respective sera with certain cancers differed from that of normal sera. The specific radioactivities of hybrid IRMA did not disappear on washing with a reaction mixture containing Triton X-100 as a detergent. Treatment of the sample with neuraminidase or periodate diminished the specific bound radioactivities, similar to CA 19-9 antigen. Furthermore, the treatment of CEAs by PI-PLC had no effect on the radioactivities. Taken together, it was suggested that CEA sugar moieties contain CA 19-9 like epitope(s).

Antigens, Tumor-Associated, Carbohydrate↗
PubMed1989

[Cholesterol atheroembolic renal failure after arteriography. Report of a case diagnosed by renal biopsy].

A case of atheroembolic renal failure diagnosed by renal biopsy was presented. A 69-year-old man was referred because of progressive renal failure two months after major angiography for occlusive arterial disease of lower limbs. The physical examination on admission revealed an uncontrollable hypertension. The laboratory findings showed elevated serum creatinine (7.5 mg/dl) and eosinophilia (1022/mm3) with normal urinalysis findings. Renal biopsy disclosed a occlusive lesion of the arcuate artery which contained cholesterol clefts and foam cells, and showed ischemic renal parenchymal changes. These findings were compatible with cholesterol atheroembolic renal disease. In spite of the aggressive medical treatment, renal function had deteriorated progressively and the patient has been on regular hemodialysis. Atheroembolic renal failure after arteriography have been reported recently, but the case diagnosed by renal biopsy has been rare. Since there is no therapeutic way to reverse this type of renal failure, strict selection of patients for the angiographic examination and use of flexible catheter might be mandatory. Subacute course of renal failure after angiography and eosinophilia seem to be the important diagnostic clues for this disorder.

Aged↗
PubMed1988

Similarity of the sugar moiety of human alkaline phosphatases between the kidney cortex and duodenum, or medulla and ileum.

Characteristics of human renal cortex and medulla alkaline phosphatase (ALP) were compared. Enzymatic and hydrophobic properties of both ALPs were almost similar. However, the results of concanavalin A affinity chromatography and wheat germ agglutinin affinity electrophoresis, exhibited that sugar chain structure(s) might be different between the cortex and medulla ALPs. In addition, the molecular mass and substrate specificity differed from each other, and these results of cortex and medulla ALPs were well accordant with those of human duodenal and ileal ALPs, respectively, as described previously (Clin Chim Acta 1987;163:279-287).

Adult↗
PubMed1988

Organ specific properties for human urinary alkaline phosphatases.

We have re-evaluated the isolation and characteristics of human urinary alkaline phosphatases (ALPs). From the results of physicochemical properties and immunological identification, the urinary ALPs from healthy subjects and patients with hepatoma were found to be similar in nature to liver and/or bone-like ALP. In patients with chronic or acute nephritis, the ALPs contained a major band of kidney-like ALP with a minor band of bone and intestinal ALPs. However, the ALPs in pregnant women had not only liver and bone ALPs but also placental-like ALP. It is interesting that only bone-like ALP was detected in psychiatric patients administered chlorpromazine. In the conditions we investigated, the molecular sizes of the urinary ALPs were similar as those of original ALPs, except for the enzyme from renal failure. Moreover, the total activity of urinary ALP was closely related to the level of serum ALP, being in a ratio of 1/40. In general, urinary ALP may be derived from serum ALP by minor modification, suggesting that the identification of excreted ALP in urine is a good marker for disturbed organs in respective diseases.

Adult↗
PubMed1988

Chlorpromazine alters bone metabolism of rats in vivo.

The acute effect of chlorpromazine (CPZ) on metabolic changes in rats was investigated. CPZ was found to markedly suppress 45Ca incorporation into the calvarium and ileum in vitro. According to the serum and/or urinary levels of certain markers for bone metabolism, the increases of Ca and P in the serum and Ca, P, and gamma-carboxyglutamate (Gla) in the urine were observed in rats given 10 mg CPZ/kg of their body weight, whereas the amount of alkaline phosphatase (ALP) activity, ionized Ca, calcitonin, 25-hydroxyvitamin D3 (25(OH)D3), 1,25-dihydroxyvitamin D3 (1,25(OH)2D3), and 24,25-dihydroxyvitamin D3 (24,25(OH)2D3) as clearly or slightly reduced, suggesting the inhibitory effect of their bone formation. This was well supported since only bone type ALP was detected in the urine and loss of the vertebral bone density from rats given daily CPZ administration for a week. Moreover, in this case, there is little if any difference in the levels of mid-molecule parathyroid hormone (mid-PTH), osteocalcin, and urinary cAMP for the nontreated and CPZ-treated animals, resulting in the fact that CPZ may mainly inhibit the hydroxylase for active vitamin D3.

1-Carboxyglutamic Acid↗
PubMed1987

Blood appearance of rat alkaline phosphatase originating from the duodenum in vitro.

The major source of rat serum alkaline phosphatase (ALP) is well known to be from the intestinal enzyme, but it is still unclear whether it is from the duodenal or the ileal enzyme. The organic origin was investigated by means of two-dimensional electrophoresis. Major isoelectric points and molecular masses for activities of duodenal enzyme treated with both phosphatidylinositol-specific phospholipase C and neuraminidase were identified apparently with those of the major serum enzyme. In organ culture, the normal duodenal enzyme was released in the highest amounts to the culture medium. These results indicate that the major source of serum ALP in adult rats is basically from the duodenal enzyme. On the other hand, lectin affinity chromatography for ALPs showed that the ALP in the medium from culture duodenum and liver had the same complex-type sugar chain as with the ALP in the duodenal tissue. Although the duodenal ALP induced by glucosamine in vitro had the hybrid-type chain, sugar chains of the induced ALP in the culture medium were of the complex type, indicating that medial ALPs possessing the same sugar chain as the native duodenal enzyme, complex type, are mainly released from their tissues in normal conditions.

Alkaline Phosphatase↗
PubMed1987

Partial characterization of human ileal alkaline phosphatase: differences between human ileal and duodenal enzymes.

Properties of human ileal and duodenal alkaline phosphatase (ALP) were compared. The pH optimum, Km values, heat stability, inhibition of activity by amino acids, and antigenicity of ileal and duodenal ALPs were similar. Affinity for DEAE and Tyraminyl derivatives/Sepharose chromatographies, substrate specificity, molecular mass, isoelectric point, and sugar chain structure differed, suggesting two forms of intestinal enzyme. The N-terminal amino acid sequence, or peptide mapping or both suggest that the two major intestinal ALPs are identical, but the minor ALP may be differed from the sequence of major one.

Alkaline Phosphatase↗
PubMed1987

Sugar-chain heterogeneity of human alkaline phosphatases: differences between normal and tumour-associated isozymes.

The sugar-chain heterogeneity of alkaline phosphatases (ALPs) from various human organs was investigated by using the serial lectin affinity technique. This technique revealed a possible structure of the sugar chain(s) of ALP isozymes and clarified a difference in affinity on the lectin column not only among three genetically different isozymes (liver/bone/kidney, intestinal and placental types) but also among liver, bone, and kidney ALPs. Lectin-binding profiles of ALPs in these human organs closely resembled those in the corresponding organs of the rat, as reported previously, suggesting that heterogeneities in sugar chains of ALPs have a specificity for the respective organs rather than being species-specific. Lectin-binding profiles of tumour-produced placental and liver ALPs were significantly different from those of ALPs in the respective normal organs. However, the two altered ALPs exhibited similar lectin-binding affinities. Isoelectric focusing analysis showed essentially no difference in protein charge between the normal and tumor-produced ALPs. Moreover, tumour-produced ALPs had the same N-terminal amino acid sequence and peptide mapping as normal ALPs. From these results, it is possible to suggest that organ-specific sugar chains in ALP isozymes are changed into those peculiar to tumours in association with malignant transformation.

Alkaline Phosphatase↗
PubMed1987

Molecular nature of three liver alkaline phosphatases detected by drug administration in vivo: differences between soluble and membranous enzymes.

1. Activities of alkaline phosphatase, liver-membranous, liver-soluble and serum-soluble, were dramatically induced in dogs by treatment with both phenobarbital and brovanexine. The treatment induced a 17-fold increase in membranous, a 155-fold increase in soluble, and a 105-fold increase in serum alkaline phosphatases. 2. There was no difference in the enzymatic behavior of the three forms of alkaline phosphatase, on heat stability, amino acid inhibition and optimum pH. 3. When the three alkaline phosphatases were treated initially with n-butanol, their apparent molecular size was identical. After treatment with phosphatidylinositol-specific phospholipase C, the liver-soluble and serum-soluble alkaline phosphatase were of the same molecular size. Liver-membranous alkaline phosphatase, however, was larger in molecular size than the other two forms, suggesting a difference between soluble and membranous alkaline phosphatase forms. 4. In terms of the sugar moiety of the three alkaline phosphatase forms, the membranous enzyme showed more of the higher affinity fraction and less of the lower affinity fraction of concanavalin A, compared with the soluble enzymes. 5. Consequently, it is possible that the membranous enzyme may be solubilized by an enzyme such as phosphatidylinositol-specific phospholipase C and modify further the sugar moiety of alkaline phosphatase molecules, resulting in serum alkaline phosphatase transfer from the soluble enzyme in liver.

Alkaline Phosphatase↗