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Biomedical subjects

B Recht

Publications and source records attributed to B Recht.

8 recordsLinked to original sources
PubMed1988

Blunt liposuction cannula dissection with and without suction-assisted lipectomy in reconstructive surgery.

Efforts continue to expand the role of blunt liposuction cannulae in flap elevation and reconstructive surgery. Suction-assisted lipectomy to reduce the actual volume of fat tissue present may allow the further reach and compressibility of mobilized flaps. These instruments find the safest possible plane for continued undermining dissection even at great distances. Applications yet unknown await discovery.

Adult↗
PubMed1986

Stress, symmetry, and psoriasis: possible role of neuropeptides.

The role of stress as a triggering factor in the exacerbation of psoriasis and the clinically symmetric distribution of psoriatic plaques suggested a possible role for neuropeptides in the etiopathogenesis of psoriasis. Several observations by other investigators involving substance P suggested to us a possible role for substance P as a modulator of the inflammatory response in psoriasis. A hypothesis for the role of substance P that would account for the temporal onset with stress, the clinical symmetry of lesions, and the histopathologic features of psoriasis is presented.

Diseases in Twins↗
PubMed1986

A bullous variant of Kaposi's sarcoma in an elderly female.

We report the case of Kaposi's Sarcoma (KS) in an elderly Italian female that has slowly progressed and evolved clinically with bullous formation. The skin biopsy was diagnostic of KS, showing the typical spindle cell formations, but at the same time showing a labyrinth-like collection of vessels that correlated with the bullous nature of the clinical lesions. Immunohistochemical staining for factor VIII antigens demonstrated strong reactivity of non-neoplastic blood vessel endothelium but virtually no staining of tumor cells. This is similar to the reactivity of normal lymphatic endothelial cells and supports the notion that these labyrinth-like vessels are derived from lymphatic endothelium.

Aged↗
PubMed1982

Staphylococcal protein A and human IgG subclasses and allotypes.

Staphylococcal protein A binds molecules belonging to the IgG1, IgG2, and IgG4 subclasses. IgG3 proteins generally do not bind, except for those coded by the two gamma 3 alleles, which are G3m(u-): G3m(b0,b3,b5,s,v). G3m(u) is located in the CH2 domain. The difference between G3m(u-) and G3m(u+) IgG3 proteins correlates with the sequence at position 339 in the CH2 domain--Ala and Thr respectively. There is another structural difference in the CH3 domain which correlates with protein A binding and non-binding: all IgG proteins that bind protein A have His at position 435, whereas those that do not, have Arg at that position.

Alleles↗
PubMed1981

Structural studies of a human gamma 3 myeloma protein (Goe) that binds staph protein A.

The partial amino acid sequence of the Fc region of an unusual monoclonal immunoglobulin molecule (Goe), which had the allotypic markers Gm (b0, b3, b5, s, t, v), rarely encountered in Caucasians, was determined. Protein Goe was previously shown to belong to the gamma 3 subclass by antigenic typing, to possess a gamma 3-like hinge region and a gamma 1-like carboxy-terminal octadecapeptide, and to bind to staphylococcal protein A. The sequence of protein Goe resembled that of gamma 3 molecules except for the presence of tyrosine at position 296, alanine at position 339, and histidine and tyrosine at positions 435 and 436. It is of interest that histidine 435 appears to play an important role in binding to Staph protein A. Since tyrosine and phenylalanine at 296 and 300 are typical of G3m(g) molecules, whereas protein Goe is G3m(g-), this may correspond to the non-b1 allotypic marker. Of the numerous explanations to account for these findings, the most likely possibilities are that protein Goe is either a hybrid molecule or the product of a germ line gene representing the G3m s allotype, which is rare in Caucasians and common in Mongoloid populations. Support for the latter alternative is provided by the isolation from normal serum of a small amount of a protein having many of the properties of protein Goe.

Chemical Phenomena↗
PubMed1977

The interaction of immunoglobulin heavy and light chains in the absence of the VH domain.

Recent studies of the micron- and kappa-chains of the first patient (GLI) with micronHCD indicated that the observed defect was the result of the failure of assembly of the intact kappa-chain to the micron-chain, which lacked the VH domain but had the CH1 Cys normally linked to the light chain. To explore the possibility that the VH region is necessary for the formation of the HL disulfide bond, in vitro studies were performed with GLI micron- and kappa-chains and with the CH1 domain and kappa-chain derived from an IgG3 myeloma protein, KUP, which yields separate VH, CH1, and kappa-chains after papain digestion and reduction. The proteins were reduced and allowed to reoxidize, and the combination products were assessed by gel chromatography under dissociating conditions by SDS-PAGE and by immunoprecipitation techniques. The results suggest that, although in vitro covalent and noncovalent combinations are possible between intact light chains and their autologous heavy chains even in the absence of the VH domain, the efficiency is less than that when the intact Fd region is used. Hence, it seems likely that lack of VH alone is not sufficient to explain the failure of assembly observed in muHCD.

Binding Sites, Antibody↗
PubMed1977

Selective proteolysis of the J chain component in human polymeric immunoglobulin.

To clarify the losses that have been observed in the J chain portion of human IgM and IgA, were carried out studies on the enzymatic susceptibility of the J polypeptide. When Waldenström macroglobulins and myeloma IgA polymers were subjected to limited proteolysis with various endopeptidases, only subtilisin was found to attack the J chain component. The pattern of cleavage was a function of the polymer species. The J chain in IgM was highly susceptible to digestion, quantitative cleavage being achieved at very low enzyme to IgM ratios and without significant changes in the remaining pentamer structure. Analyses of the digestion products showed that the initial cleavage occurred at an exposed region midway in the J sequence and was followed by extensive degradation of the carboxy-terminal segment. These findings indicated that the observed loss of the IgM J component can be explained by the inadvertent introduction of subtilisin in vitro or by the attack of in vivo enzymes with a specificity similar to subtilisin. In contrast, the IgA J chain was found to be much more resistant to subtilisin proteolysis; its cleavage required higher enzyme concentrations and was accompanied by significant degradation of the alpha-chains. Thus, it appears unlikely that the IgA J polypeptide is degraded by either in vitro or in vivo enzymes unless its accessibility is first enhanced by changes in the IgA Fc structure.

Amino Acid Sequence↗