Receptor For Acylation Stimulating

PROTEIN (C3A-DESARG)? 159

Kay Johswich and Andreas Klos

1 Introduction 159

2 The C5L2 receptor 160

2.1 C5L2 as a Member of the Anaphylatoxin Receptor Family 160

2.2 Postulated functions of C5L2 164

3 C5L2 and Lipid and Carbohydrate Metabolism 164

3.1 The Adipsin / ASP Model 164

3.2 Historical Development of the Adipsin/ASP Model 165

3.3 C5L2 as a Receptor for ASP? 169

3.4 Critical Evaluation of Experimental Findings 170 3.4.1 Quality of Purified ASP, Recombinant ASP and Synthetic

Peptides as Stimuli, and Biologic Activity of ASP 170

3.4.2 Binding Data (Calculated Kd) - and Recent Results Indicating that C5L2 is not the Receptor for ASP 171

3.4.3 Receptor Dependent or Independent Functional Responses and Intracellular Signal Transduction ? 172

3.4.4 Determinations and Concentrations of ASP (or C3) in Human

Serum and Observations in Humans and Animals 172

4 C5L2 as an Anti-inflammatory Molecule 174

References 176

13. THE EXOSPORIUM OF B.CEREUS CONTAINS A BINDING SITE FOR gC1qR/p33: IMPLICATION IN SPORE

ATTACHMENT AND/OR ENTRY* 181

Berhane Ghebrehiwet, Lee Tantral, Mathew A. Titmus, Barbara J. Panessa-Warren, George T. Tortora, Stanislaus S. Wong, John B. Warren

Abstract 181

1 Introduction 181

2 Materials and Methods 183

2.1 Chemicals and reagents 183

2.2 Expression of recombinant gC1qR/p33 183

2.3 Monoclonal antibodies 184

2.4 Binding studies 184

2.5 Phagocytosis assay 184

2.6 Preparation of carbon nanoloops 185

2.7 Preparation of cells for microscopic analyses 185

2.8 Microscopic analyses 186

2.8.1 Light microscopy 186

2.8.2 Electron Microscopy 186

3 Results 187

3.1 The binding of gC1qR to B. cereus is temperature and calcium dependent 187

3.2 EDTA abrogates gC1qR binding to B. cereus 187

3.3 Neutrophils and monocytes readily take up B. cereus spores 188

3.4 Electron microscopic analyses 189

4 Discussion 192

5 Acknowledgements 195

6 Abbreviations 195 References 195

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