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Biomedical subjects

B Goldberg

Publications and source records attributed to B Goldberg.

At least 199 records · Page 11Linked to original sources
PubMed1973

Antibodies to a precursor of human collagen.

Antiserum prepared against serum-free medium from human fibroblast cultures reacted specifically with protropocollagen, an assembled, soluble precursor of tropocollagen. The antibodies were directed to antigenic determinants in the nonhelical, amino terminal peptide extensions (propeptides). Amino acid sequences in the precursor molecule corresponding to the telopeptides and helical alpha chains of tropocollagen were not recognized by the antiserum.

Antibodies↗
PubMed1973

Secretion and extracellular processing of procollagen by cultured human fibroblasts.

Cultures of human diploid fibroblasts were labeled with radioactive proline and glycine, and the precursor of collagen (procollagen) in cells and medium was characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A covalently assembled molecule with the composition (pro alpha1)(2).pro alpha2 (approximate molecular weight, 360,000) appeared intracellularly soon after synthesis of the constituent chains, and could be detected in the medium after 60 min of labeling. The molecule was stabilized by disulfide bonds between cysteine residues in the amino-terminal procollagen peptide sequences of the three chains. Collagenase digested the molecule to peptides of 30,000 molecular weight or less. Limited digestion with pepsin excised nonhelical procollagen peptides, yielding native, triple-helical tropocollagen. Pulse-chase experiments indicated that a peptidase in the medium sequentially excised the nonhelical peptides from the molecule, generating tropocollagen molecules that aggregated as fibers in the cell layer. The excised, nonhelical procollagen peptides contained little or no proline or glycine. Intramolecular bonds of the lysyl aldehyde type were not detected in the secreted molecule, as reduction of the medium always resulted in quantitative recovery of free pro alpha chains in dodecyl sulfate-urea. Lysyl-derived, covalent bonds appeared to form between tropocollagen molecules aggregating in the cell layer. We suggest the term "pro-tropocollagen" for the assembled, secreted precursor of collagen.

Carbon Isotopes↗
PubMed1972

Analgesic nephropathy.

Sixty-six patients were seen from January 1963 to December 1970 in whom a diagnosis of analgesic nephropathy was made. The ratio of women to men was 2.7:1 and women presented at an earlier age. Over 60% of patients had or developed urinary tract infection and over one-third presented with serum urea levels over 300 mg/100 ml. Hypertension was present in 60% of patients and almost 20% had a history of peptic ulcer; hysterectomy had been done in 35% of the women. Most patients improved initially but more than half of those followed up died within five years of presentation. A direct relation was found between prognosis and the degree of functional renal impairment at presentation. Hypertension appeared to have an adverse effect on prognosis but no relation of prognosis to papillary necrosis, infection, or surgical procedures was found.

Adult↗
PubMed1972

Precursors of collagen secreted by cultured human fibroblasts.

Soluble precursors of collagen ("procollagens") in the culture medium of human diploid fibroblasts were characterized by molecular sieve chromatography on 6% agarose and by sodium dodecyl sulfate-acrylamide gel electrophoresis. Under the denaturing conditions for gels, the following molecular species were identified: a major species of three procollagen chains, a procollagen dimer, and free procollagen chains. Reduction with 2-mercaptoethanol completely dissociated the trimer and dimer, releasing procollagen alpha1 and procollagen alpha2 chains with molecular weights of about 120,000. Both pro alpha1 and pro alpha2 chains could be labeled with [(35)S]cystine. In addition, free procollagen chains with molecular weights of less than 120,000, but heavier than native alpha chains, were identified in gels. Radioactivity in all of the above molecules could be chased into native alpha chains extracted from extracellular fibers of the cell layers. The data indicate that: (i) collagen is secreted as a disulfidestabilized procollagen trimer with the composition, (pro alpha1)(2).pro alpha2; (ii) noncovalent interactions maintain the three-chain assembly during stepwise enzymatic excisions of N-terminal, cysteine-containing procellagen peptides; and (iii) after such excisions, native helical molecules, (alpha1)(2).alpha2, precipitate as fibers in the cell layers.

Carbon Isotopes↗
PubMed1970

Tissue typing, antilymphocyte globulin, and prophylactic graft irradiation in cadaver kidney transplantation.

In a series of 27 recipients of cadaver kidney grafts, 26 were at the time of writing alive, 3 to 25 months after transplantation, and 25 patients were alive with functioning first grafts. The one-year patient survival in 18 patients was 94% and the one-year graft survival was 89%. There was no beneficial correlation between tissue matching and the frequency of major early rejection episodes or graft function 12 or more months after transplantation. Antilymphocyte globulin administration was associated with a lower incidence of early rejection episodes, but this was not statistically significant. A combination of prophylactic graft irradiation and antilymphocyte globulin administration for at least the first two weeks was associated with a significantly reduced frequency of major early rejection episodes and appreciably better graft function at 12 months. This effect could not be ascribed to better tissue matching.

Antilymphocyte Serum↗