William P. Kolb

BD Biosciences (United States)

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Hans J. Müller‐Eberhard

Bernhard Nocht Institute for Tropical Medicine

Eckhard R. Podack

University of Miami

Gale A. Granger

Illumina (United States)

Linda M. Kolb

The University of Texas Health Science Center at Houston

Rick A. Wetsel

The University of Texas Health Science Center at Houston

John S. Sundsmo

Stellar Biotechnologies (United States)

John D. Tamerius

Quidel Corporation (United States)

Joseph H. Lang

Education & Research Foundation

R. Neal Pinckard

The University of Texas Health Science Center at San Antonio

Jay R. Savary

Response Technologies (United States)

Cooperative Institutions

Scripps Health

Scripps Clinic

The University of Texas Health Science Center at San Antonio

University of California, San Diego

National Institutes of Health

University of Washington

Banner Sun Health Research Institute

University of North Carolina at Chapel Hill

New York University

The University of Texas Health Science Center at Houston

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Lymphocyte in vitro cytotoxicity: Characterization of mouse lymphotoxin

Cellular Immunology (1970)

William P. Kolb Gale A. Granger

Lymphotoxin alpha

10.1016/0008-8749(70)90065-1

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Citations (70)

New neo-epitope specific ELISA kits to determine anaphylatoxin C3adesArg and C5adesArg levels in biological fluids

Immunopharmacology (2000)

Julia A. Ember Stephanie Windman Feng Jun Luan Sharon Sasaki Liangru Shi

Anaphylatoxin

10.1016/s0162-3109(00)80269-6

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Citations (0)

C1Q receptors on cultured human gingival fibroblasts: analysis of binding properties.

The Journal of Immunology (1983)

Sandra Bordin William P. Kolb R. Page

The interaction of the purified C1q component of human C with synchronized, quiescent human gingival fibroblasts was investigated, and the presence of a specific binding site was demonstrated. Quantitative binding studies with radioiodinated C1q showed that binding was specific, saturable, and reversible upon addition of unlabeled C1q or by increasing the salt concentration. Scatchard plot analysis of the data yielded an affinity constant of 2 X 10(7) M-1 for all cell strains examined. The capacity for C1q binding varied among the eight cell strains examined. The number of binding sites per cell ranged from 2.6 to 17.7 X 10(6) with an average of 8.4 X 10(6). The receptor was insensitive to trypsin digestion, and it bound the collagen-like portion of the C1q molecule. Specific immunofluorescence staining showed that virtually all the viable cultured fibroblasts were able to bind added C1q. Flow cytometric analysis demonstrated a spectrum of fluorescence intensity among the cell strains, and there was a positive correlation between fluorescence intensity and the number of binding sites detected by using radiolabeled C1q.

Immunofluorescence

Scatchard plot

Binding constant

10.4049/jimmunol.130.4.1871

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Citations (73)

Measurement of SC5b-9 in urine in patients with the nephrotic syndrome

Kidney International (1991)

James L. Ogrodowski Lee A. Hebert Daniel D. Sedmak Fernando G. Cosio John D. Tamerius

Membranous Nephropathy

Nephritis

Urine collection device

10.1038/ki.1991.326

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Citations (81)

LYMPHOCYTE ACTIVATION AND LYMPHOTOXIN PRODUCTION

Elsevier eBooks (1971)

William P. Kolb Terry W. Williams Gale A. Granger

10.1016/b978-0-12-107750-1.50027-3

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Citations (8)

Waveguide CO 2 lasers for a space communications transceiver (A)

Journal of the Optical Society of America A (1976)

Thomas F. Johnston William P. Kolb Ian Ramsay Carolina Romero

Transceiver

Waveguide

Free-Space Optical Communication

Source

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The C5b-6 Complex: Formation, Isolation, and Inhibition of Its Activity by Lipoprotein and the S-Protein of Human Serum

The Journal of Immunology (1978)

Eckhard R. Podack William P. Kolb Hans J. Müller‐Eberhard

Abstract C5b-6 complex was generated by activation of C7-depleted serum and purified 1200-fold based on its hemolytic activity. A homogeneous bimolecular complex with an s-rate of 11.5S and a m.w. of 328,000 daltons was obtained. The electrophoretic mobility was -3.4 × 10-5 cm2/volt sec. The subunit composition as revealed by SDS-polyacrylamide electrophoresis without reduction showed two protein bands: C5b (180,000) and C6 (120,000); and with reduction three subunits: C6 (128,000), C5bα (122,000), and C5β (75,000). Immunochemical analysis confirmed complex formation between C5b and C6 and showed the presence of one of the two neoantigens expressed by the SC5b-9 complex. Sixty nanograms of C5b-6 represented 108 hemolytically effective molecules. A hemolytic efficiency of 12 to 20 C5b-6 cell-bound complexes per lytic event was calculated from the uptake of radiolabeled C5b-6. The hemolytic efficiency of C5b-6 is dependent on the cell concentration. C5b-6-initiated lysis is strongly inhibited by serum low density lipoproteins with an inhibition constant of Ki = 34 µg/ml and by the S-protein with Ki = 39 µg/ml. Lipoproteins and S-protein form a stable, hemolytically inactive complex with nascent C5b-7. The mechanism of C5b-7 inhibition is interpreted as a competition reaction between the target cell membrane and the inhibitors for the transitory binding site in nascent C5b-7.

Lytic cycle

10.4049/jimmunol.120.6.1841

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Citations (151)

Complement-dependent induction of DNA synthesis and proliferation of human diploid fibroblasts

Journal of Cellular Physiology (1980)

Terry I. Korotzer James Clagett William P. Kolb Roy C. Page

Abstract The effects of fresh human serum (FHS) and heat‐inactivated human serum (HHS) on the DNA synthesis and proliferation of human diploid fibroblasts were assessed. FHS activated significantly more quiescent fibroblasts to undergo DNA synthesis and proliferation than did HHS. The stimulatory effect occurred consistently over a serum concentration range of 0.1–10%. Using bromodeoxyuridine selective killing techniques, it was shown that this FHS stimulatory effect was on a specific subpopulation of fibroblasts unresponsive to HHS. The involvement of the complement system, and specifically of C1, was shown by the inability of Clq‐depleted FHS to support enhanced DNA synthesis whereas Clq‐depleted serum reconstituted with purified Clq was effective. Purified Clq did not restore activity when added to heated serum, nor was it mitogenic when tested in basal medium without serum. The addition of purified Clq to fresh serum inhibited the enhancement of DNA synthesis, and at Clq concentrations of 4γ/ml and greater, the fresh serum effects were abrogated. Thus, it appears that binding of the assembled C1 complex to the fibroblast surface was required for FHS‐mediated enhancement of fibroblast proliferation, with Clq subcomponent serving as the recognition site. The results from several experiments indicated that antibody was not required for the complement‐dependent fibroblast activation. FHS was not cytotoxic, and autologous serum was as effective as allogeneic sera. A 20‐fold molar excess of Fab' from pooled human IgG did not alter the FHS effects. FHS from which IgG was more than 99% depleted was still effective. These results suggested an antibody‐independent role for complement in the activation of a subpopulation of human diploid fibroblasts.

Microgram

WI-38

Bromodeoxyuridine

10.1002/jcp.1041050314

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Citations (30)

Quantitation and stability of the fifth component of complement (C5) in bronchoalveolar lavage fluids obtained from non-human primates.

PubMed (1981)

William P. Kolb Linda M. Kolb Rick A. Wetsel Walter R. Rogers James O. Shaw

The functional activity and antigenic expression of the fifth component of complement (C5) in concentrated bronchoalveolar lavage fluids (BALF) and serum samples obtained from 13 nonsmoking and 13 smoking baboons was quantified by specific hemolytic titration and radioimmunoassays. The number of C5H505 units per milligram of albumin in BALF obtained from nonsmoking and smoking baboons indicated a nearly 2-fold increase in C5 hemolytic activity in lavage fluids as compared to matched serum samples. No significant differences (p greater than 0.05) in C5 hemolytic or antigenic (radioimmunoassay) expression were evident between BALF samples obtained from nonsmoking and smoking baboons. C5 stability in BALF was indicated by the highly significant correlation (p less than 0.005) between C5 hemolytic activity and antigenic expression. The absence of C5-cleaving enzymes in BALF was verified by incubation of 125I-C5 with these fluids, followed by SDS5 polyacrylamide slab gel and autoradiographic analyses. These results demonstrated the presence and stability of substantial quantities of functionally active C5 in the secretions of primate lungs, which represents a readily available source of phlogistic fragments for the initiation of pulmonary inflammation.

Complement component 5

10.1164/arrd.1981.123.2.226

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Citations (31)

THE MEMBRANE ATTACK MECHANISM OF COMPLEMENT

The Journal of Experimental Medicine (1973)

William P. Kolb Hans J. Müller‐Eberhard

The membrane attack mechanism of complement, C5 to C9, has previously been postulated to associate on the target cell surface to a stable decamolecular complex with a calculated mol wt of 995,000. A soluble and stable complex consisting of C5, C6, C7, C8, and C9 has now been demonstrated to arise as a consequence of complement activation by the classical or alternate pathway. It has a sedimentation coefficient of 22.5S and a mol wt of 1 million daltons, and it migrates on electrophoresis at pH 8.6 as an alpha-globulin. The stable and soluble C5b-9 complex cannot bind to erythrocytes and has no demonstrable cytolytic activity. However, due to partially unsaturated binding sites for C9, it can bind additional C9 and thus function as an inhibitor of lysis of EAC1-8 by C9. These results support the concept according to which the membrane-bound attack system of complement represents a stable, decamolecular assembly of C5b-9. Unlike its analogue in free solution, the membrane-bound complex is cytolytically active.

Complement

10.1084/jem.138.2.438

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Citations (111)