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Biomedical subjects

K I Kim

Publications and source records attributed to K I Kim.

At least 55 records · Page 3Linked to original sources
PubMed1997

Students' stress in China, Japan and Korea: a transcultural study.

In this transcultural comparison of stress among Chinese, Japanese and Korean students, the authors examined stressors with the Stress Questionnaire Form for College Students, strategies for coping with Ways of Coping-Revised, and physical reactions to the stressors with the Physical Symptom Scale of Stress. Compared to the Japanese and Korean students, Chinese students had a multitude of stressors and experienced the highest level of stress. In coping with stressful events, Koreans were the most active, Chinese the least active and Japanese were intermediately active. Physical symptoms were found to be most serious in Koreans and less serious in Chinese and Japanese. Coping techniques seemed unrelated to alleviating physical symptoms in Koreans but mildly related in Chinese and Japanese.

Adaptation, Psychological↗
PubMed1997

Pulmonary carcinosarcoma: radiologic and pathologic findings in three patients.

OBJECTIVE: The purpose of this study was to describe the radiologic and pathologic features of pulmonary carcinosarcoma in three patients. CONCLUSION: The tumors measured 9-14 cm in diameter, had inhomogeneous contrast enhancement, and in two cases had invaded the mediastinum or chest wall extensively. Carcinosarcomas are rare tumors that tend to be large, necrotic, enhancing, and locally invasive.

Adult↗
PubMed1997

Basal cell adenocarcinoma of the salivary gland--a case report.

Basal cell adenocarcinoma of the salivary gland is a very rare disease entity as the malignant counterpart of basal cell adenoma. On the basis of morphologic pattern, basal cell adenoma can be divided into four subtypes; trabecular, solid, tubular, and dermal analogue (membranous). We report a case of basal cell adenocarcinoma in the left parotid gland of a 33-year-old woman. Light microscopically, the tumor cells were composed of relatively uniform, monotonous basaloid cells. The tumor cell nests commonly had peripheral palisadings. The main growth pattern of the tumor cells was tubulotrabecular. However, other portions were similar to dermal analogue monomorphic adenoma and showed cribriform patterns reminiscent of adenoid cystic carcinoma. The tumor had frequent perineural invasions and an infiltrative margin. On immunohistochemistry, only scattered numbers of tumor cells showed irregular positive reaction for S-100 protein, suggesting a few myoepithelial cell components of the tumor compared with most tumor cells derived from epithelial cells.

Adenocarcinoma↗
PubMed1997

A case of intraductal papillary tumor of pancreas associated with mucinous ductal ectasia.

Intraductal papillary neoplasm associated with mucinous ductal ectasia is an uncommon cystic disease of the pancreas. This tumor is characterized by the multilocular cyst lined by mucin producing cells with variable degrees of atypia and ductal ectasia. In addition, this tumor has a favorable prognosis in contrast to other mucinous cystic tumor of the pancreas. Reports on intraductal mucin producing tumor are quite limited and most of them are found in Japanese literature. We report a case of intraductal papillary adenocarcinoma with marked dilatation of the pancreatic duct filled with mucin in a 72-year-old female patient.

Adenocarcinoma, Mucinous↗
PubMed1995

Purification and characterization of protease Ci, a cytoplasmic metalloendoprotease in Escherichia coli.

Protease Ci, a cytoplasmic metalloprotease in Escherichia coli, has been purified to apparent homogeneity by conventional chromatographic procedures using 125I-labeled oxidized insulin B-chain as a substrate. The purified enzyme behaves as a 54-kDa protein under both denaturing and nondenaturing conditions, suggesting that it consists of a single polypeptide chain. It is inhibited by metal-chelating agents, including o-phenanthroline and NaCN, but not by inhibitors of serine proteases or thiol-blocking agents. Furthermore, protease Ci was found to contain 1.1 mol of zinc per mol of the enzyme upon analysis by HR ICP mass spectroscopy. Thus, protease Ci must be a zinc metalloprotease. Among the polypeptides tested as substrates, oxidized insulin B-chain and glucagon are most rapidly hydrolyzed. Intact insulin is a much poorer substrate than oxidized insulin B-chain, even though the affinity of the enzyme to intact insulin is approximately 100-fold greater than that to the B-chain. Since unlabeled oxidized insulin A-chain is capable of inhibiting the hydrolysis of 125I-labeled insulin B-chain, it also appears to be a substrate. Protease Ci also degrades lysozyme and lactalbumin, although to a much lesser extent than oxidized insulin B-chain. However, it shows little or no activity against proteins larger than 15 kDa (e.g. ovalbumin and denatured bovine serum albumin). Hydrolysis of oxidized insulin B-chain followed by amino acid composition analyses of the cleavage products reveals that as many as 10 of its 29 peptide bonds are hydrolyzed by protease Ci. This ability to hydrolyze relatively small polypeptides suggests that protease Ci may catalyze the later steps in the pathway for intracellular protein breakdown.

Amino Acid Sequence↗
PubMed1995

Comparison of nuclear bone and gallium scans in the therapeutic evaluation of bone lymphoma.

The objective of this study was to compare Tc-99m MDP bone and Ga-67 scans for the therapeutic response to bone lymphoma in 40 patients. The authors retrospectively compared 40 Tc-99m MDP bone scans and 20 Ga-67 scans before therapy, 29 bone scans and 13 Ga-67 scans during the therapy, and 33 bone scans and 15 Ga-67 scans after therapy. Tc-99m MDP and Ga-67 whole body scans were obtained within 2 weeks of each study and were graded visually (grades 1-4) in which grade 3 means similar count density to that of normal iliac alar activity on bone scans and normal liver activity on Ga-67 scans, respectively. The findings of lesion improvement during and after therapy were found in 66.0% (19 of 29) and 72.7% (24 of 33) with Tc-99m MDP bone scans, 84.6% (11 of 13) and 86.7% (13 of 15) with Ga-67 scans, respectively. The mean grades of Tc-99m MDP uptake were 3.06 before, 2.34 during, and 1.75 after therapy. The mean grades of Ga-67 uptake were 3.22 before, 1.42 during, and 1.30 after therapy. Ga-67 scans appear to be more reliable than Tc-99m MDP bone scans in evaluating the therapeutic response of bone lymphoma.

Adult↗
PubMed1994

The 65-kDa protein derived from the internal translational initiation site of the clpA gene inhibits the ATP-dependent protease Ti in Escherichia coli.

The clpA gene that encodes the ATPase subunit of the ATP-dependent protease Ti (Clp) in Escherichia coli contains a putative internal translational initiation site. Here we show that mutagenesis of its 5'-end AUG codon resulted in an exclusive synthesis of the 65-kDa protein (ClpA65), while mutation at the internal 169th AUG codon (Met) to ACG (Thr) produced only the 84-kDa protein (ClpA84T). On the other hand, the cells carrying the wild-type clpA gene produced both the 84- and 65-kDa proteins (ClpA84/65). While the purified ClpA84T and ClpA84/65 hydrolyzed ATP nearly as well as the 84-kDa ClpA alone (ClpA84), ClpA65 cleaved ATP at a rate less than 5% of that by ClpA84. Unlike ClpA84 and ClpA84T, ClpA65 could not support the casein-degrading activity of ClpP. Furthermore, ClpA65 inhibited the proteolysis by the mixture of ClpP with ClpA84 or ClpA84T but not that with ClpA84/65, which could support the proteolytic activity of ClpP only about 40% as well as ClpA84. Nevertheless, ClpA65 showed little or no effect on the basal or protein-activated ATPase activity of ClpA84, ClpA84T, or ClpA84/65 alone or in the presence of ClpP. These results suggest that ClpA65 may interfere the interaction of ClpA84 or ClpA84T with ClpP and, hence, impair their assembly into an active form of the ATP-dependent protease Ti.

Adenosine Triphosphatases↗
PubMed1993

Site-directed mutagenesis of the dual translational initiation sites of the clpB gene of Escherichia coli and characterization of its gene products.

The heat shock protein ClpB in Escherichia coli is a protein-activated ATPase and consists of two proteins with sizes of 93 and 79 kDa. By polymerase chain reaction-aided site-directed mutagenesis, both the proteins have been shown to be encoded by the same reading frame of the clpB gene, the 93-kDa protein (ClpB93) from the 5'-end AUG translational initiation site and the 79-kDa protein (ClpB79) from the 149th codon (an internal GUG start site). Both the purified ClpB93 and ClpB79 proteins behave as tetrameric complexes with a very similar size of about 350 kDa upon gel filtration on a Superose-6 column. Both appear to be exclusively localized to the cytosol of E. coli. Both show inherent ATPase activities and have an identical Km of 1.1 mM for ATP. The ATPase activity of ClpB93 is as markedly stimulated by proteins, including casein and insulin, as that of wild-type ClpB, but the same proteins show little or no effect on ClpB79. Because ClpB79 lacks the 148 N-terminal sequence of ClpB93 but retains the two consensus sequences for adenine nucleotide binding, the N-terminal portion appears to contain a site(s) or domain(s) responsible for protein binding. Furthermore, ClpB79 is capable of inhibiting the casein-activated ATPase activity of ClpB93 in a dose-dependent manner but without any effect on its inherent ATPase activity. In addition, ClpB93 mixed with differing amounts of ClpB79 behave as tetrameric molecules, although its protein-activated ATPase activity is gradually reduced. These results suggest that tetramer formation between ClpB93 and ClpB79 may be responsible for the inhibition of the activity.

Adenosine Triphosphatases↗
PubMed1993

Schizophrenic delusions among Koreans, Korean-Chinese and Chinese: a transcultural study.

In this transcultural study of schizophrenic delusions among Koreans, Korean-Chinese and Chinese, many delusions were shown to be different among the three groups in their frequency and content and the differences could be explained by sociocultural and political factors. Delusional themes sensitive to influence by sociocultural or political situations and changes seem to be 'family', 'love affairs', 'religious matters', 'economic matters', 'specific physical damage' and 'political themes.' Delusions about 'family', 'love affair', 'being raped', 'religious matters' and 'economic and business matters' were most frequent in Koreans. Delusions of 'blood-relatedness', 'longevity' and 'political themes' were most frequent in Korean-Chinese. Delusions of 'bloodsucking and brain or viscera extracted' and 'poison or being pricked by poisoned needle' were most prominent in Chinese.

Adult↗
PubMed1993

Structure and properties of the 26S protease complex from chick skeletal muscle.

The 26S protease complex was purified from chick skeletal muscle and shown to consist of unusually heterogeneous 21-140 kDa polypeptides, including the 21-32 kDa subunits of the 20S proteasome. Electron microscopic analysis revealed that the 26S complex may have a symmetric morphology with two large rectangular terminal domains attached to a thinner central 20S proteasome domain. The 26S complex was capable of degrading the peptide substrates of the 20S proteasome, including Suc-LLVY-AMC, N-Cbz-LLE-NA and N-Cbz-ARR-MNA. The two enzyme complexes showed similar sensitivities to various site-specific protease inhibitors, although their sensitivities to SDS were differed from each other. Immunoprecipitation with anti-26S complex antibody reduced peptide hydrolysis by the 20S proteasome. Similarly, anti-20S proteasome antibody inhibited peptide hydrolysis by the 26S complex. These results demonstrate that the 26S protease complex contains the 20S proteasome as a functional and structural component.

Amino Acid Sequence↗
PubMed1992

The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase.

The clpB gene in Escherichia coli encodes a heat-shock protein that is a close homolog of the clpA gene product. The latter is the ATPase subunit of the multimeric ATP-dependent protease Ti (Clp) in E. coli, which also contains the 21-kDa proteolytic subunit (ClpP). The clpB gene product has been purified to near homogeneity by DEAE-Sepharose and heparin-agarose column chromatographies. The purified ClpB consists of a major 93-kDa protein and a minor 79-kDa polypeptide as analyzed by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Upon gel filtration on a Superose-6 column, it behaves as a 350-kDa protein. Thus, ClpB appears to be a tetrameric complex of the 93-kDa subunit. The purified ClpB has ATPase activity which is stimulated 5-10-fold by casein. It is also activated by insulin, but not by other proteins, including globin and denatured bovine serum albumin. ClpB cleaves adenosine 5'-(alpha,beta-methylene)-triphosphate as rapidly as ATP, but not adenosine 5'-(beta,gamma-methylene)-triphosphate. GTP, CTP, and UTP are hydrolyzed 15-25% as well as ATP. ADP strongly inhibits ATP hydrolysis with a Ki of 34 microM. ClpB has a Km for ATP of 1.1 mM, and casein increases its Vmax for ATP without affecting its Km. A Mg2+ concentration of 3 mM is necessary for half-maximal ATP hydrolysis. Mn2+ supports ATPase activity as well as Mg2+, and Ca2+ has about 20% their activity. Anti-ClpB antiserum does not cross-react with ClpA nor does anti-ClpA antiserum react with ClpB. In addition, ClpB cannot replace ClpA in supporting the casein-degrading activity of ClpP. Thus, ClpB is distinct from ClpA in its structural and biochemical properties despite the similarities in their sequences.

Adenosine Triphosphatases↗
PubMed1983

Determination of amino acid requirements of young pigs using an indicator amino acid.

Mixtures of skim milk and free amino acids were compared as diets for pigs which would allow manipulation of dietary amino acid levels. Piglets gained 208 g/d between 3 and 14 d of age on the skim-milk diet, but replacement of 600 g/kg of the dietary nitrogen with free amino acids reduced growth rate to 148 g/d. Supplementation of a lysine-deficient diet with lysine reduced the catabolism of [14C]phenylalanine showing that phenylalanine catabolism could be used as an indicator of the adequacy of diet with respect to another essential amino acid. The dietary level of phenylalanine which would provide an excess for catabolism by the piglet was estimated directly by measuring the influence of dietary phenylalanine level on [14C]phenylalanine oxidation. Reduction of the dietary phenylalanine level below 7 g/kg had no effect on phenylalanine oxidation, whereas increasing the dietary phenylalanine level above 7 g/kg resulted in a linear increase in phenylalanine oxidation. An indirect estimate of histidine requirement was made by examining the influence of dietary histidine level on [14C]phenylalanine oxidation. In diets containing more than 4 g histidine/kg, phenylalanine oxidation was minimal. In diets containing less than 4 g histidine/kg, [14C]phenylalanine oxidation increased as the level of dietary histidine was reduced. This showed that the utilization of the essential amino acid phenylalanine, for protein synthesis, was not limited by histidine supply in diets containing more than 4 g histidine/kg. A direct estimate of histidine requirement was made by examining the influence of dietary histidine level on [14C]histidine oxidation. Diets with more than 4 g histidine/kg contained an excess which was catabolized: there was a linear increase in histidine oxidation in response to dietary histidine levels greater than 4 g/kg. This confirmed the previous indirect estimate of histidine requirement.

Amino Acids↗
PubMed1983

Amino acid oxidation by young pigs receiving diets with varying levels of sulphur amino acids.

Piglets were weaned at 3 d of age and were introduced to liquid diets in which 400 g/kg protein was supplied as skim-milk powder and the balance as a mixture of free amino acids. The skim milk contributed 2.3 g methionine and 1.4 g cystine/kg diet; the experimental diets were made by supplementing these levels with free amino acids. The adequacy of the test level of the amino acid in the diet was assessed by measuring the oxidation of [1-14C]phenylalanine as an indicator of the partition of the essential amino acids between incorporation into protein and degradation. Radioactivity recovered as carbon dioxide was used as a measure of catabolism. Addition of 0.2, 0.4, 0.7, 1.2 and 1.7 g L-methionine/kg to a diet containing 5 g cystine and 3 g choline chloride/kg showed that phenylalanine catabolism was minimal for the diet with 2.7 g methionine/kg indicating that this is the dietary requirement for methionine to serve as a source of methionine residues for protein synthesis. Addition of D-methionine to produce a series of diets with graded levels of methionine showed that the D-isomer was less effective than the L-isomer in reducing phenylalanine catabolism: the addition of 0.8 g D-methionine/kg diet was needed to produce the same effect as 0.4 g L-methionine/kg diet showing that the replacement value of D-methionine for L-methionine was 50% in the young pig.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acids↗
PubMed1983

Oxidation of an indicator amino acid by young pigs receiving diets with varying levels of lysine or threonine, and an assessment of amino acid requirements.

The catabolism of [14C]phenylalanine was used to indicate the effects of varying the dietary level of lysine and threonine on the retention of dietary amino acids by 2-week-old pigs receiving diets containing skim milk and a mixture of free amino acids. Reducing the dietary level of lysine from 16 to 12 g/kg had no influence on phenylalanine oxidation, reducing the lysine level from 12 to 11 then to 10 g/kg caused an almost linear increase in phenylalanine oxidation whereas further reduction to 9 or 8 g/kg resulted in a less-marked increase in phenylalanine oxidation. This showed that 12 g lysine/kg was required to maximize amino acid retention and indicated that lysine was conserved more effectively at low dietary concentrations than at dietary concentrations approaching the requirement. Reducing the dietary level of threonine from 8 to 6 g/kg had no influence on phenylalanine oxidation, whereas further reduction to 4 g/kg caused a linear increase in phenylalanine catabolism showing that 6 g threonine/kg was required to maximize amino acid retention. Reduction of the levels of lysine, threonine and methionine from the generous levels characteristic of a diet containing 240 g protein from skim milk/kg, to the requirement levels determined separately in the presence of the generous levels of all the other amino acids, resulted in a twofold increase in phenylalanine catabolism. This shows that the pig seems able to conserve limiting intakes of a single amino acid, but not if the intakes of two or three amino acids are limiting.

Animals↗