Biomedical subjects
A Dorfman
Publications and source records attributed to A Dorfman.
Extrapolating movement without retinal motion.
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DSM-III-R personality disorders in parents of schizophrenic patients.
This study examines the frequency of DSM-III-R personality disorders in parents of 58 patients who were admitted consecutively to a New York State psychiatric hospital with a first admission for a schizophrenia-like psychosis. For comparison, a control group of 65 families were randomly recruited who were in the same age group and denied any psychiatric history in their immediate families. Significantly more parents of the patients had a diagnosed personality disorder than controls. These were classified as schizoid, schizotypal, histrionic, and sadistic types by DSM-III-R criteria. While paranoid personality disorder was frequent, it was equally distributed among both groups of parents. These data suggest that the genetic boundaries to a "schizophrenia spectrum" disorder may extend further than previously thought and particularly the specific characteristics that are common to a wide variety of these disorders need to be examined in further analyses.
The language of art--a byzantium of words.
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Familial thyroid disease and delayed language development in first admission patients with schizophrenia.
One hundred consecutive first admission patients with a DSM-III-R diagnosis of schizophrenia, schizoaffective disorder, or schizophreniform disorder were compared with 100 randomly selected community controls. Childhood histories of physical, medical, and perinatal trauma, as well as physical and cognitive development, were examined by structured interviews with all available mothers of patients and controls. The prevalence of specific psychiatric disorders and several medical illnesses among first degree and more distant relatives was determined by family history questionnaires. The patient group did not have an excess of childhood head injuries, serious infections, or perinatal/birth complications compared with controls. With social class level taken into account, it was found that the acquisition of reading skills occurred significantly later in patients than controls. Family histories of schizophrenia and thyroid disorders were significantly more frequent among patients than controls. These data fail to indicate any childhood physical or medical environmental trauma that could lead to an increased risk for schizophrenia, although patients were substance abusers to a greater extent than controls. This study also confirms the already known contribution of familial factors and suggests an association of the inheritance of thyroid disorders with schizophrenia. Delayed development of reading skills suggests that precursers of illness may appear early in life before psychosis is evident.
Regression modeling of consumption or exposure variables classified by type.
Consumption or exposure variables, as potential risk factors, are commonly measured and related to health effects. The measurements may be continuous or discrete, may be grouped into categories and may, in addition, be classified by type. Data analyses utilizing regression methods for the assessment of these risk factors present many problems of modeling and interpretation. Various models are proposed and evaluated, and recommendations are made. Use of the models is illustrated with Cox regression analyses of coronary heart disease mortality after 24 years of follow-up of subjects in the Framingham Study, with the focus being on alcohol consumption among these subjects.
Cell-free translation of messenger RNA for chondroitin sulphate proteoglycan core protein in rat cartilage.
Total RNA was extracted from the cartilage tissues rat Swarm chondrosarcoma, neonatal-rat breastplate and embryonic-chicken sterna and translated in wheat-germ cell-free reactions. The core protein of the chondroitin sulphate proteoglycan subunit was identified among translation products of rat mRNA by its apparent Mr of 330 000 and by its immunoprecipitation with specific antisera prepared against rat or chicken proteoglycan antigens. The apparent Mr of the rat proteoglycan core protein is 8000-10000 less than that of the equivalent chicken cartilage core-protein product.
Construction and partial characterization of recombinant cDNA clones for chicken type I collagen messenger RNAs.
Messenger RNAs for the alpha 1 and alpha 2 chains of type I procollagen were partially purified from total embryonic chicken calvaria using gel chromatography on Sepharose 4B and used to construct recombinant cDNA clones corresponding to both mRNAs. Restriction site mapping, nucleotide sequencing and hybridization to RNA blots were used to show that clones pCAL1 and pCAL2 contain inserted sequences corresponding to the mRNAs for chicken alpha 1 and alpha 2 procollagen chains, respectively.
Identification of genomic DNA coding for chicken type II procollagen.
A segment of the type II procollagen gene has been isolated by screening a lambda Charon 4A library containing fragments of chicken genomic DNA. The specific clone, LgCOL(II), was selected by hybridization using overlapping inserts from two cDNA clones which are specific for a cartilage procollagen (Vuorio, E., Sandell, L., Kravis, D., Sheffield, V. C., Vuorio, T., Dorfman, A., and Upholt, W. B. (1982) Nucleic Acids Res. 10, 1175-1192). DNA sequence analysis of LgCOL(II) in the COOH-telopeptide region of the protein, shows conclusively that this DNA corresponds to the chicken type II procollagen gene. Hybridization of cDNA probes to restriction fragment gel blots together with DNA sequence analysis have established the orientation and position of the procollagen gene within the lambda Charon 4A vector and indicate that LgCOL(II) contains approximately 6 kilobase pairs of the type II procollagen gene plus additional DNA flanking the 3' end of the gene. DNA sequence analysis shows directly that LgCOL(II) contains DNA sequences identical with those in the cDNA clones. The portion of the gene from amino acid 578 of the triple helical region to the COOH-terminal end of the protein (approximately 700 amino acids) is contained within the clone, corresponding to approximately 50% of the amino acid coding sequence of the gene. This region of the chicken alpha 1 (type II) procollagen gene is encoded within a shorter segment of the chicken genome than is the corresponding region of the alpha 2(type I) procollagen gene.
Construction and partial characterization of two recombinant cDNA clones for procollagen from chicken cartilage.
Type II procollagen mRNA has been partially purified from embryonic chick sternal cartilage by guanidine hydrochloride extraction, sucrose gradient sedimentation and Sepharose 4B chromatography. Double stranded cDNA was synthesized using AMV reverse transcriptase and E. coli DNA polymerase I, tailed using terminal transferase and inserted into the Pst I site of pBR322. Two putative type II procollagen cDNA clones have been characterized. Both plasmids hybridize to 2 sternal RNA species, a major species of 5.3 kb and a minor species of 7 kb. These RNAs are present in total RNA from sterna and differentiated limb bud cultures but are not detected in RNA from stage 24 limb bud which has not yet differentiated to cartilage or in RNA from calvaria. The time of appearance of these RNAs during the differentiation of limb mesenchyme in culture parallels the appearance of translatable type II procollagen mRNA.
The irreversible effect of bromodeoxyuridine on chick chondrocytes.
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Gene expression during chick limb cartilage differentiation.
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Chondroitin 6-sulfate oligosaccharides as immunological determinants of chick proteoglycans.
Monoclonal antibodies to hyaluronidase-treated chondroitin sulfate proteoglycan (CSPG) were used to study the immunological determinants of chick cartilage proteoglycan. The determinants recognized by the antibodies were studied by a radioimmune inhibition assay utilizing hyaluronidase-treated [35S]CSPG. Hyaluronidase-treated CSPG inhibits the reaction of four clonal antibodies, S54C, S103L, S11D, and P100D, with [35S]CSPG, but to varying degrees. Only the reaction of S103L is inhibited to a considerable extent by undigested CSPG, indicating that hyaluronidase treatment exposes determinants specific for the other three antibodies. These findings are consistent with the earlier conclusion that S103L is specific for a protein determinant (Dorfman et al., 1980). Only the reaction of S54C is not significantly inhibited by chondroitinase ABC-digested CSPG. This result indicates that chondroitinase ABC digestion can also expose determinants recognized by S11D and P100D but that such digestion removes the determinant recognized by S54C. Of the four antibodies tested, only the reaction of S54C with hyaluronidase-treated [35S]CSPG is significantly inhibited by chondroitin-6-SO4 tetra- and hexasaccharide (59 and 43% inhibition, respectively, at a concentration of 1333 microM). The reaction of S54C is inhibited to a lesser extent by chondroitin tetra- and hexasaccharide (28 and 26% inhibition, respectively, at a concentration of 1333 microM). In contrast, chondroitin-4-SO4 oligosaccharides do not inhibit the reactions of any of the clonal antibodies. These result suggest that S54C recognizes a determinant that contains chondroitin-6-SO4 oligosaccharide, attached via the linkage oligosaccharide to core protein.
Nothing fails like success.
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Chemical and immunological characterization of proteoglycans of embryonic chick calvaria.
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Structural and associative properties of cartilage matrix constituents in mice with hereditary chondrodysplasia.
The disarray of proliferative chondrocytes in epiphyses of cho/cho mice has been attributed to a defect in the extracellular matrix. Histochemically and ultrastructurally the matrix gives the appearance that it lacks the necessary structural integrity to guide proliferating cells into columns essential to elongation of endochondral bones. A study of rib cartilage was conducted to determine if the abnormality might be due to a defect in structural or associative properties of either of the two major matrix constituents, chondroitin sulfate proteoglycan (CSPG) or type II collagen. The molecular weights of guanidine-extracted proteoglycan (PG) and of protease-released chondroitin sulfate (CS) were not different from those of controls. Chondroitinase digestion of [3H]glucosamine-labeled CS yielded normal ratios of sulfated:nonsulfated disaccharides. Upon addition of hyaluronate to the PG extract there was normal interaction between these two macromolecules. Collagen was determined to be type II and contained normal amounts of glycosyl and hydroxyl residues. Incorporation rates of labeled precursors of both CSPG and collagen were normal suggesting that the abnormality does not involve differences in rate of synthesis of these macromolecules. These data provide evidence that the genes involved with the synthesis and posttranslational modification of proteoglycan and collagen are not affected by a mutation at the cho locus.
Cell-free translation of cartilage RNAs.
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Immunological methods in the study of chondroitin sulfate proteoglycans.
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