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Biomedical subjects

M W Cunningham

Publications and source records attributed to M W Cunningham.

71 records · Page 4Linked to original sources
PubMed1988

Eccrine porocarcinoma.

Eccrine porocarcinoma is a rare malignancy of the eccrine sweat duct unit. This article brings to 79 the number of cases reported. Our report and a review of the literature illustrate the natural history and pathological findings of this disease. Patients' ages at the time of appearance for treatment range from 19 to 90 years. The lesions show no predilection for site; their location follows the distribution of sweat glands in the body. Thirty-nine percent of all patients had cutaneous, regional lymph node, or visceral metastases. Primary treatment is wide surgical excision. The value of adjunctive therapy has not been proved.

Adenocarcinoma↗
PubMed1988

Monoclonal antibodies to Pasteurella haemolytica serotype 1 lipopolysaccharide: demonstration of antigenic similarities among several serotypes.

Murine monoclonal antibodies (MAbs) were produced which were specific for Pasteurella haemolytica serotype 1 lipopolysaccharide (LPS). The MAbs also reacted with LPS present in a partially purified antigen derived from a saline extract of the organism. The epitope to which the MAbs were directed was a carbohydrate which was sensitive to oxidation with periodate, had a molecular weight between 14,000 and 25,000 as determined by immunoblotting, and was present in a crude O-antigen preparation of P. haemolytica LPS. The MAbs did not react with purified capsular polysaccharide from P. haemolytica serotype 1. In an enzyme-linked immunosorbent assay, reaction of the MAbs with LPS obtained from 14 gram-negative bacteria failed to detect any cross-reactivity with P. haemolytica LPS. However, the MAbs detected antigenic similarities among P. haemolytica serotypes 1, 5, 6, 7, 8, and 12 and, to a lesser extent, 4 and 14. These studies indicate that the LPS-O-antigens from several P. haemolytica serotypes have similar epitopes and may be partially responsible for shared antigenicity among serotypes.

Animals↗
PubMed1987

Nonocclusive ischemic colitis secondary to hemorrhagic shock.

A young male with a penetrating chest wound suffered modest and transitory hemorrhagic shock. Nonocclusive right-sided ischemic colonic necrosis developed secondarily. This became obvious on serial follow-up examinations, prompting exploration and curative surgical resection. This case represents ischemic colitis secondary to hemorrhagic shock following trauma. Upon review of the literature, only five other such cases have been reported. Although shock-associated ischemic colitis is well documented, it is extremely uncommon to see gangrenous changes of the bowel in young, otherwise healthy, trauma victims. Mesenteric vasospasm is believed to be the causative factor in these cases. For unknown reasons, the right colon seems to be the favored site of ischemic damage. Nonocclusive intestinal ischemia should be considered in patients who have abdominal pain after a hypotensive episode.

Adult↗
PubMed1986

Polyspecificity of antistreptococcal murine monoclonal antibodies and their implications in autoimmunity.

mAbs produced by immunization of BALB/c mice with Streptococcus pyogenes M type 5 membranes were further characterized for their reaction with S. pyogenes pep M5 protein and with autoantigens associated with human cell lines. mAbs 36.2.2 and 54.2.8 simultaneously reacted with M protein and a membrane protein(s) of S. pyogenes. When cell lines were mixed with 54.2.8, we saw nuclear fluorescence along with staining of the cytoskeleton. Subsequent experiments revealed that 54.2.8 was an anti-DNA antibody that reacted with DNA, poly(I), poly(dT), and weakly with cardiolipin. Its reactivity with the cytoskeleton could be blocked with anti-vimentin. On the other hand, 36.2.2 reacted with the cytoskeleton, sparing the nucleus, and was inhibited by the alpha helical proteins myosin, actin, and keratin. mAb 54.2.8 was inhibited with myosin, but not with actin and keratin. None of the antibodies studied were inhibited by collagen, and none of them were rheumatoid factors. The results imply that Group A streptococci can activate B cell clones against myosin, alpha helical proteins, or DNA, thereby contributing to the enhancement of autoantibody production.

Animals↗
PubMed1986

Monoclonal antibodies cross-reactive with group A streptococci and normal and psoriatic human skin.

Infection with group A streptococci has been implicated as a factor capable of exacerbating psoriasis. In order to explore the possibility of cross-reactivity between streptococcal antigens and human skin in this phenomenon, skin from psoriatic patients and control subjects was reacted with 3 monoclonal antibodies against group A streptococci and antibody binding was estimated by the indirect immunofluorescence technique. Monoclonal antibody 54.2.8 stained the nuclei and cytoplasm of cells within the epidermis and epidermal appendages, as well as cells scattered throughout the dermis. In contrast, monoclonal antibodies 49.8.2 and 36.2.2 labeled the cytoplasm of epidermal cells and epidermal appendages but did not react with nuclei. No difference in the staining patterns of control skin and uninvolved skin from patients with psoriasis was observed. However, skin from psoriatic lesions contained large amounts of cross-reactive skin component(s). Sera from patients with guttate psoriasis did not react differently with normal or psoriatic skin when compared with normal sera. Western immunoblots of skin extracts demonstrated that monoclonal antibody 54.2.8 reacted with a family of proteins in the molecular weight range of 60-70K. The results indicate that component(s) in human skin share cross-reactive epitopes with group A streptococci. Immunologic cross-reactions between group A streptococci and human skin may play an important role in the exacerbation of certain skin disorders following streptococcal infections.

Adolescent↗
PubMed1986

A study of anti-group A streptococcal monoclonal antibodies cross-reactive with myosin.

Anti-group A streptococcal monoclonal antibodies were obtained from BALB c/BYJ mice immunized with purified membranes from M type 5 Streptococcus pyogenes. Two of the anti-streptococcal monoclonal antibodies were previously shown to cross-react with muscle myosin. In this study the monoclonal antibodies were reacted with tissue sections of normal human heart and skeletal muscle. Antibody binding was estimated by indirect immunofluorescence and immunoperoxidase techniques. Both of the monoclonal antibodies (36.2.2 and 54.2.8) investigated in this report reacted with heart and/or skeletal muscle sections. When evaluated by immunofluorescence, monoclonal antibody 54.2.8 demarcated the periphery of cardiac striated muscle cells and reacted to a lesser degree with subsarcolemmal components. Monoclonal antibody 36.2.2 failed to react with heart sections, but both of the monoclonal antibodies reacted strongly with skeletal muscle sections. Results similar to those observed with indirect immunofluorescence were obtained with the immunoperoxidase technique. By Western immunoblotting and competitive inhibition assays, monoclonal antibodies 36.2.2 and 54.2.8 both were found to react with the heavy chain of skeletal muscle myosin. However, only 54.2.8 reacted with the heavy chain of cardiac myosin. The specificity of the monoclonal antibodies for subfragments of skeletal muscle myosin indicated that monoclonal antibody 36.2.2 was specific for light meromyosin fragments, whereas 54.2.8 reacted with both heavy and light meromyosin. The data demonstrated that two monoclonal antibodies against streptococci were specific for skeletal muscle and/or cardiac myosin and for subfragments of the myosin molecule. The reactions of the monoclonal antibodies with human tissue sections were consistent with the immunochemical reactions of the monoclonal antibodies with both denatured and native myosin.

Animals↗
PubMed1985

Myosin: a link between streptococci and heart.

Murine monoclonal antibodies to Streptococcus pyogenes reacted with skeletal muscle myosin. High molecular weight proteins in extracts of human heart tissue that reacted with an antibody to S. pyogenes also reacted with a monoclonal antibody to ventricular myosin. Adsorption of the antibody to streptococci with S. pyogenes simultaneously removed reactivity of the antibody for either S. pyogenes or myosin. These results indicate that myosin shares immunodeterminants with a component of S. pyogenes.

Animals↗
PubMed1985

The vascular supply to the proximal interphalangeal joint.

Four methods were used to identify the vascular branches that supply the proximal interphalangeal joint in 55 cadaver fingers. They were intra-arterial injection of radiopaque dyes, microscopic dissections of the arterial system, selective injection of specific branches followed by sectioning of the joints and examination of the areas stained, and histologic sectioning. Our studies show that the major branches of the digital artery to the joint arise from the dorsal aspect of the vessel, while smaller branches that run to the soft tissue arise from the palmar side. Three branches supply the proximal interphalangeal joint. The first arises 1.5 to 2.5 cm proximal to the joint and divides into branches to the dorsal skin, the bone proximally, the vincular system, the lateral surface of the joint, and the palmar plate. The other two branches arise distal to the joint space; the first has branches to the palmar aspect of the joint of the middle phalanx and the vincular system. The most distal of the three perfuses the dorsal surface of the joint.

Arteries↗
PubMed1985

Retardation of finger growth after injury to the flexor tendons.

The absence of any part of the total mechanical force (i.e., flexor tendons) may be responsible for retardation of bone growth during a child's growth phase. The cause of retardation may be dedifferentiation of cartilage cells at the epiphyseal plate. Four cases in which unrepaired flexor tendons in digits caused retardation of growth illustrate this possible phenomenon. We feel that this is not a well recognized problem and thus deserves mention to stimulate further study. We believe that meticulous primary repair in children is desirable not only to preserve function, but also to prevent growth disturbances.

Age Factors↗
PubMed1984

Determining the recipient site for a sensory island pedicle.

When performing a sensory island transfer for restoration of sensibility to an area of pinch, one must be accurate in determining the recipient site. We present a simple and precise means of determining the recipient site for a sensory island transfer by ink-blotting the areas of contact of the thumb and index finger.

Amputation, Traumatic↗
PubMed1984

Aquaplast for nasal splinting.

A nasal splint ideally should be sturdy, moldable, light, easy to apply, and inconspicuous. Plaster, dental compound, and aluminum are currently used but each has limitations. We have found that Aquaplast, a material softened by immersion in hot water, more closely conforms to the qualities of the ideal nasal splint. Aquaplast is sturdy, light, thin, very moldable, easy to apply, and allows for passage of air and moisture.

Female↗
PubMed1984

Murine monoclonal antibodies reactive with human heart and group A streptococcal membrane antigens.

Ten selected murine hybridoma cell lines that produce monoclonal antibodies against M type 5 Streptococcus pyogenes and human heart antigen were isolated. All of the monoclonal antibodies studied were determined to be the immunoglobulin M isotype. The antibodies were characterized on the basis of their reactions with Triton X-100-extracted whole human heart antigens, sodium dodecyl sulfate-extracted sarcolemmal antigens, and whole streptococci or their membranes. Enzyme-linked immunosorbent assays and Western immunoblotting techniques were used to compare the reactivity of the monoclonal antibodies. All 10 of the antibodies were first selected for their reactivity with Triton X-100-extracted heart antigens and whole group A, M type 5 streptococci. These antibodies were then divided into two categories: strong reactors or weak reactors with human sarcolemmal and streptococcal membranes. Among the strong reactors, two different types of monoclonal antibodies were observed on the basis of their immunobanding patterns with sarcolemmal and streptococcal membranes on Western blots. Monoclonal antibodies that were strong reactors with sarcolemmal and group A streptococcal membrane antigen were directed against a determinant on a family of proteins. The major reactants of sarcolemmal extracts were high-molecular-weight proteins near 200,000. Some monoclonal antibodies demonstrated more specificity for the heart than did others when reacted with separated Triton X-100-extracted tissue antigens from the heart, kidney, and skeletal muscle. One of the monoclonal antibodies that reacted with group A streptococci reacted with a Triton X-100-extracted heart antigen ca. 40,000 daltons in size. None of these monoclonal antibodies opsonized type 5 Streptococcus pyogenes, and in enzyme-linked immunosorbent assays most of the antibodies were found to react to a lesser degree with other groups of streptococci. Monoclonal antibody was used to probe normal and rheumatic sarcolemma for differences in reactivity. Although the rheumatic heart reacted more intensely, no major differences between the immunobanding patterns of normal and rheumatic hearts were observed.

Animals↗
PubMed1983

Study of heart-reactive antibody in antisera and hybridoma culture fluids against group A streptococci.

Heart-reactive antibody is known to be produced in animals immunized with group A streptococci. However, the detection and quantitation of these antibodies and their respective antigens have been limited to immunofluorescence or immunoprecipitation tests. In this study a more sensitive technique was used to detect heart-reactive antibody, i.e., the enzyme-linked immunosorbent assay (ELISA). Countercurrent immunoelectrophoresis and agar gel immunodiffusion were also used to confirm the reactivity of rabbit antisera to group A streptococci and human heart tissue. Human heart tissue antigen was prepared by Triton X-100 extraction, and checkerboard titrations of heart tissue antigen versus streptococcal antisera revealed optimal concentrations of each for the ELISA. When immune rabbit serum was reacted with heart tissue antigen, a 5- to 10-fold increase was observed over the reactions of preimmune sera controls. Streptococcal antiserum was found to have a six- to eightfold greater reactivity with heart tissue antigen than with similar concentrations of kidney and skeletal muscle antigens. Heart tissue antigen was partially purified by DEAE-cellulose chromatography, and quantities of greater than 10 to 100 ng (dry weight) were shown to react with streptococcal antisera in the ELISA. Heart, kidney, and skeletal muscle antigens were subjected to electrophoresis in polyacrylamide gel slabs and blotted onto a nitrocellulose filter. These filter blots reacted with streptococcal antisera and confirmed the tissue antigen specificity observed with the ELISA. In addition, the ELISA was found to be an effective method for the detection of heart-reactive antibodies produced by murine hybridomas that were producing antibody to group A streptococci.

Antibodies, Bacterial↗
PubMed1983

Response of an abdominal aortic thrombotic occlusion to local low-dose streptokinase therapy.

Local low-dose streptokinase infusion (5000 to 6000 IU/hr) as compared to systemic streptokinase infusion (loading dose 250,000 IU/hr, maintenance dose 100,000 IU/hr) successfully relieved a total thrombotic abdominal aortic occlusion. No complications of bleeding or distal embolization occurred during streptokinase therapy, which required only 8 days of hospitalization. When seen at 4 months after streptokinase infusion, the patient was still free of symptoms. When no immediate threat of ischemic limb loss exists, streptokinase may offer a promising therapeutic alternative to surgical intervention for patients who represent a poor operative risk.

Aorta, Abdominal↗
PubMed1974

Peptic digestion of streptococcal M protein. I. Effect of digestion at suboptimal pH upon the biological and immunochemical properties of purified M protein extracts.

Purified streptococcal M protein vaccines often produce non-type-specific immunotoxic reactions in the skin or the blood of humans. In an attempt to free the type-specific M antigen (TSM) of such non-type-specific (NTSM) immunotoxic properties, purified M protein preparations were subjected to brief periods (5 to 10 min) of enzymatic digestion in dilute solutions of pepsin (20 mug/ml) at pH 5.0. Such peptic digestion abolished the ability of M protein to aggregate platelets in human platelet-rich plasma and to precipitate plasma fibrinogen. It greatly reduced (up to 16-fold) the capacity of M protein to react with the NTSM complement-fixing antibody that is normally present in human serum. In contrast, it had no effect upon the reactivity of the type-specific M antigen; the pepsin-treated M protein retained its ability to inhibit type-specific streptococcal opsonization by homologous M antibody, and, moreover, retained its ability to elicit type-specific opsonic antibody responses in rabbits.

Antibody Formation↗