Search PubMed⌕ Search

Biomedical subjects

Y L Chan

Publications and source records attributed to Y L Chan.

At least 145 records · Page 8Linked to original sources
PubMed1990

The primary structure of rat ribosomal protein S16.

The amino acid sequence of rat ribosomal protein S16 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. S16 contains 145 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has a molecular mass of 16,304. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 11-13 copies of the S16 gene. The mRNA for the protein is about 700 nucleotides in length. Rat S16 is homologous to mouse S16 (there are 2 amino acid changes and a residue is deleted) and related to Halobacterium morismortui ribosomal protein S3 and to Escherichia coli S9.

Amino Acid Sequence↗
PubMed1990

The primary structure of rat ribosomal protein S24.

The amino acid sequence of rat ribosomal protein S24 was deduced from the sequence of nucleotides in a recombinant cDNA. S24 contains 133 amino acids and has a molecular mass of 15,413. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 12-16 copies of the S24 gene. The mRNA for the protein is about 600 nucleotides in length. Rat S24 is homologous to Xenopus laevis S19 and related to Halobacterium morismortui ribosomal protein S15.

Amino Acid Sequence↗
PubMed1990

RNA-protein interaction. An analysis with RNA oligonucleotides of the recognition by alpha-sarcin of a ribosomal domain critical for function.

alpha-Sarcin is a cytotoxic protein that inactivates ribosomes by hydrolyzing a single phosphodiester bond on the 3' side of G-4325 in eukaryotic 28 S rRNA. We have examined the requirements for the recognition by alpha-sarcin of this domain using a synthetic oligoribonucleotide (35-mer) that reproduces the sequence and, we presume, the secondary structure (a stem, a bulged nucleotide, and a loop) at the site of modification. The wild type structure and a large number of variants were transcribed in vitro from synthetic DNA templates with phage T7 RNA polymerase. Recognition of the substrate is strongly favored by a G at the position that corresponds to 4325. There is an absolute requirement for a helical stem; however, it can be reduced from the 7 base pairs in the natural structure to 3 without loss of specificity. The nature of the base pairs in the stem modifies but does not abolish recognition; whereas, the bulged nucleotide does not contribute to identification. Cleavage is materially affected by altering the nucleotides in the universal sequence surrounding G-4325 and changing the position in the loop of the tetranucleotide GAG(sarcin)A leads to loss of recognition by the toxin. We propose that the alpha-sarcin domain RNA participates in elongation factor catalyzed binding of aminoacyl-tRNA and of translocation; that translocation is driven by transitions in the structure of the alpha-sarcin domain RNA initiated by the binding of the factors, or the hydrolysis of GTP, or both; and that to toxin inactivates the ribosomes by preventing this transition.

Adenosine↗
PubMed1990

Time- and dose-dependent effects of protein kinase C on proximal bicarbonate transport.

Activation of protein kinase C has been shown to cause both stimulation and inhibition of transport processes in the brush-border membrane and renal tubule. This study was designed to examine the dose-response nature and time-dependent effect of 4 beta-phorbol-12-myristate-13-acetate (PMA) on the rates of bicarbonate absorption (JHCO3) and fluid absorption (Jv) in the proximal convoluted tubule (PCT) of rat kidney. Bicarbonate flux was determined by total CO2 changes between the collected fluid and the original perfusate as analyzed by microcalorimetry. Luminal perfusion of PMA (10(-10) approximately 10(-5) M) within 10 min caused a significant increase of JHCO3 and Jv. A peaked curve of the dose response was observed with maximal effect at 10(-8) M PMA on both bicarbonate and fluid reabsorption, which could be blocked completely by amiloride (10(3) M) and EIPA (10(-5) M). On the other hand, with an increase of perfusion time beyond 15 min. PMA (10(-8) and 10(-6) M) could inhibit JHCO3 and Jv. Amiloride (10(-3) M) or EIPA (10(-5) M) significantly inhibits JHCO3 and Jv, while there is no additive effect of PMA and amiloride or EIPA on PCT transport. An inactive phorbol-ester, 4 alpha-phorbol, that does not activate protein kinase C, had no effects on JHCO3 and Jv. Capillary perfusion of PMA (10(-8) M) significantly stimulate both JHCO3 and Jv; however, PMA did not affect glucose transport from either the luminal side or basolateral side of the PCT. These results indicate that activation of endogenous protein kinase C by PMA could either stimulate or inhibit both bicarbonate and fluid reabsorption in the PCT dependent on time and dose, and these effects are through the modulation of Na+/H+ exchange mechanism.

Amiloride↗
PubMed1990

Cholinergic effect on rat proximal convoluted tubule.

The effect of cholinergic agents on proximal tubular absorption of bicarbonate and fluid were examined to investigate the possible role of the cholinergic receptor in the regulation of renal function. Proximal convoluted tubule (PCT) and peritubular capillaries were perfused with bicarbonate-Ringer's solution containing radioactive inulin. Bicarbonate (total CO2) was determined by microcalorimetry. The rates of bicarbonate absorption (JHCO3) and fluid absorption (Jv) were 143.3 +/- 7.2 pEq/min.mm and 2.52 +/- 0.23 nl/min.mm, respectively. Addition of carbachol (10(-8) M) to the capillary perfusate reduced JHCO3 by 17% and Jv by 32%. A higher dose of carbachol (10(-6) M) did not further inhibit JHCO3 or Jv. Simultaneous perfusion of atropine (10(-5) M) together with carbachol (10(-8) M) abolished the inhibitory effect of carbachol on PCT transport. Atropine itself, however, had no effect on PCT transport. The inhibitory effect of carbachol was also diminished by lanthanum chloride (10(-4) M). Carbachol (10(-6) M) had no effects from the luminal side. W-7, a calmodulin antagonist, inhibited carbachol-induced effects. Ionophore A-23187 also inhibited Jv and JHCO3. However, there was no additive effect when A-23187 and carbachol were combined in the capillary perfusate. These results suggest that there are functional cholinergic receptors on the basolateral side of the PCT that can regulate JHCO3 and Jv. Calcium influx may play a role in mediating the cholinergic effects on PCT transport.

Absorption↗
PubMed1990

The primary structure of rat ribosomal protein S3.

The amino acid sequence of rat ribosomal protein S3, which has been reported to form part of the binding site for initiation factors, was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein S3 contains 243 amino acids and has a molecular weight of 26,643. Rat S3 and Xenopus laevis ribosomal protein S1 are homologous: There are 62 identities in 63 consecutive residues in the carboxyl-terminal amino acid acid sequence of rat S3 and in a partial sequence of Xenopus S1. Hybridization of rat S3 cDNA to digests of nuclear DNA suggests that there are 8-10 copies of the S3 gene. The mRNA for the protein is about 950 nucleotides in length.

Amino Acid Sequence↗
PubMed1990

Management of a hydropic infant with congenital heart block.

A baby with congenital heart block and hydrops fetalis diagnosed prenatally was delivered at 36 weeks of gestation. Heart failure was controlled with temporary cardiac pacing which was complicated by perforation of the myocardium. She made an uneventful recovery after implantation of a permanent pacemaker. Sjögren's syndrome A antibodies were detected in her serum. Coincidentally, she also had pulmonary valvular stenosis as a structural abnormality.

Female↗
PubMed1990

Sodium and bicarbonate reabsorption in microperfused proximal tubules from the denervated rat kidney: relationship to cortical Na-K-ATPase activity.

Although numerous studies have documented the effects of the renal nerves on kidney function, the mechanisms involved in the diuresis have yet to be elucidated. The present study was undertaken to examine the effect of acute unilateral renal denervation (DNX) on proximal tubular absorption of fluid and bicarbonate and to determine if acute DNX was associated with changes in Na-K-ATPase activity. Acute DNX caused significant increases in urine flow and absolute and fractional excretions of Na, HCO3 and K compared to the contralateral control kidney (INN) or sham denervated kidneys in normal rats as well as in rats made alkalotic by the I.V. infusion of 150 mM NaHCO3. These effects were seen without significant changes in GFR. When proximal convoluted tubules (PCT) were perfused with bicarbonate-Ringer's solution DNX resulted in a 67% decrease in fluid reabsorption (INN: 3.0 +/- 0.2 vs DNX: 1.0 +/- 0.1 nl/min/mm; p less than 0.001) and a 40% decline in bicarbonate (total CO2) reabsorption (INN: 151.3 +/- 8.8 vs DNX: 94.5 +/- 10.1 pmol/min/mm; p less than 0.01). Acute DNX caused a significant reduction in Na-K-ATPase activity measured in microsomes derived from the outer cortex of the kidney (INN: 13.2 +/- 1.3 vs DNX: 10.9 +/- 0.7 mumol PO4/mg prot/hr; p less than 0.01) while Mg-ATPase was unaffected. Sham denervation had no effect on any of the above parameters. These results indicate that the renal nerves play an important role in the regulation of bicarbonate and fluid reabsorption in the PCT. The diuresis, natriuresis, and bicarbonaturia associated with acute unilateral renal denervation may be the direct result of inhibition of Na-K-ATPase activity.

Acid-Base Equilibrium↗
PubMed1990

Mechanism of angiotensin II action on proximal tubular transport.

Our previous studies have shown that a low dose of angiotensin II (Ang II) stimulates fluid and bicarbonate absorption from the apical side of rat proximal tubule (PCT). These effects can be blocked by Ang II antagonist, (Sar1, Ile8)Ang II. The cellular mechanism underlying Ang II action, however, remained unclear. Thus, this study was designed to investigate the possible role of phosphoinositide turnover in mediating this action of angiotensin. Rat PCT was perfused in vivo with Ringer's solution containing [3H]inulin as a volume marker. Bicarbonate flux (JHCO3) was determined by total CO2 changes between the collected fluid and the original perfusate as analyzed by microcalorimetry. Luminal perfusion of 10(-11) M Ang II stimulated both JHCO3 and fluid reabsorption. These effects could be blocked by 10(-3) M amiloride and 10(-5) M ethylisopropylamiloride. Luminal perfusion of 4 beta-phorbol-12-myristate-13-acetate (10(-8) M) also stimulated both fluid reabsorption and JHCO3. These effects could also be blocked by amiloride and ethylisopropylamiloride. When both Ang II (10(-11) M) and 4 beta-phorbol-12-myristate-13-acetate (10(-8) M) were perfused together, the stimulatory effects on fluid reabsorption and JHCO3 were not additive. These results suggest that Ang II interacts with its receptors on the apical membrane leading to modulation of the Na-H exchange mechanism in PCT. The phosphoinositide turnover may play an important role in the Ang II action on PCT transport.

Amiloride↗
PubMed1989

The primary structure of rat ribosomal protein L26.

The amino acid sequence of rat ribosomal protein L26 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. Rat L26 contains 145 amino acids and has a molecular mass of 17,266 Da. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 8-16 copies of the L26 gene. The mRNA for the protein is about 650 nucleotides in length. Protein L26 has a sequence of 9 residues that may be repeated in three places.

Amino Acid Sequence↗
PubMed1989

The primary structure of rat ribosomal protein L37a.

The amino acid sequence of rat ribosomal protein L37a was deduced from the sequence of nucleotides in recombinant cDNAs isolated in Yamagata and in Chicago and confirmed from the NH2-terminal amino acid sequence of the protein. Ribosomal protein L37a contains 91 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has a molecular mass of 10143 Da.

Amino Acid Sequence↗
PubMed1989

The primary structure of rat ribosomal protein L21.

The covalent structure of rat ribosomal protein L21 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. Ribosomal protein L21 contains 159 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has a molecular weight of 18,322. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 16-23 copies of the L21 gene. The mRNA for the protein is about 680 nucleotides in length.

Amino Acid Sequence↗
PubMed1989

The primary structure of rat ribosomal protein S4.

The amino acid sequence of the rat 40 S ribosomal subunit protein S4 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino-acid sequence of the protein. Ribosomal protein S4 has 282 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has a molecular weight of 31,841. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 7-11 copies of the S4 gene. The mRNA for the protein is about 1 kb in length. Rat S4 is homologous to Saccharomyces cerevisiae YS6. The protein contains a possible internal duplication of 11 residues.

Amino Acid Sequence↗
PubMed1989

The primary structure of rat ribosomal protein S10.

The amino acid sequence of rat ribosomal protein S10 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. Ribosomal protein S10 contains 165 amino acids and has a molecular mass of 18917 Da. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 17-20 copies of the S10 gene. The mRNA for the protein is about 750 nucleotides in length. Ribosomal protein S10 has several possible internal duplications; one is a tandem repeat of ten residues that is basic and contains two or three prolines.

Amino Acid Sequence↗
PubMed1989

The primary structure of rat ribosomal protein L34.

The amino acid sequence of rat ribosomal protein L34 was deduced from the nucleotide sequence in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. Ribosomal protein L34 contains 117 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has an Mr of 13,498. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 7-9 copies of the L34 gene. The mRNA for the protein is about 630 nucleotides in length.

Amino Acid Sequence↗
PubMed1989

The primary structure of rat ribosomal protein L18a.

The amino acid sequence of rat ribosomal protein L18a was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein L18a contains 175 amino acids and has a molecular mass of 20,047 Da. Hybridization of the cDNA to digests of rat nuclear DNA and to a preparation of poly(A)+ mRNA suggests that there are 8-11 copies of the L18a gene and that the mRNA for the protein is about 700 nucleotides in length. Rat L18a is related to Schizosaccharomyces pombe L17 and perhaps to Halobacterium marismortui L19.

Amino Acid Sequence↗