Nomenclature for proteins: is calprotectin a proper name for the elusive myelomonocytic protein?

Introduction "New" proteins will continue to be discovered, and suitable names for them should be sought. In many instances preliminary symbols are introduced which serve a practical purpose until the proteins have been characterised and appropriate descriptive names can be chosen. Using modem molecular biological methods, the existence of a protein may be suspected before it has ever been seen on an analytical gel. By cloning and gene manipulaton it may also be possible to produce proteins that may never appear in the human body. This raises a fundamental question: when should the specific protein be regarded as such and be given a proper name? When the DNA sequence is determined? When the specific mRNA is formed? When single polypeptides emerge from ribosomes? When glycosylated or otherwise modified polypeptides are detected within the cell? When complexes of more than one polypeptide chain are formed? Or when the functionally active substance is released? The very fact that such questions have not yet been discussed in depth in the scientific literature, let alone been covered by international conventions, suggests that the problems involved are difficult to address. In a time when biological sciences are becoming increasingly dominated by patents and their use for commercial purposes, it is not surprising that different scientific groups may be reluctant to agree that they are, in fact, working with the same protein: it might spoil the chance of obtaining a separate patent. In the case of calprotectin, which will be used as an example below, scientists have been unwilling to exchange reagents or use proper analytical methods to clarify whether various groups were working with the same protein. There is a good tradition and sound basis for giving descriptive names for well characterised, functional proteins. Their genes should also be named accordingly. As characterisation and delineation of biological activities may take considerable time, the use of preliminary symbols or short notations for proteins will still be necessary.

[1]  B. Egelandsdal,et al.  Calcium binding and concomitant changes in the structure and heat stability of calprotectin (L1 protein) , 1995, Clinical molecular pathology.

[2]  R. Lehrer,et al.  In vitro candidastatic properties of the human neutrophil calprotectin complex. , 1993, Journal of immunology.

[3]  J. Edgeworth,et al.  An immunohistochemical analysis of onchocercal nodules: evidence for an interaction between macrophage MRP8/MRP14 and adult Onchocerca volvulus , 1993, Clinical and experimental immunology.

[4]  N. Hogg,et al.  MRP‐8 and MRP‐14, two abundant Ca2+‐binding proteins of neutrophils and monocytes , 1993, Journal of leukocyte biology.

[5]  R. Lehrer,et al.  In vitro Antimicrobial Activity of the Human Neutrophil Cytosolic S-100 Protein Complex, Calprotectin, Against Capnocytophaga sputigena , 1993, Journal of dental research.

[6]  R. Christensen,et al.  The distribution of the antimicrobial protein, calprotectin, in normal oral keratinocytes. , 1992, Archives of oral biology.

[7]  A. Røseth,et al.  Assessment of the neutrophil dominating protein calprotectin in feces. A methodologic study. , 1992, Scandinavian journal of gastroenterology.

[8]  P. Mowinckel,et al.  Calprotectin (the L1 protein) during surgery in patients with rheumatoid arthritis. , 1991, Scandinavian journal of clinical and laboratory investigation.

[9]  K. Gatter,et al.  The L1 antigen and squamous metaplasia in the bladder , 1991, Histopathology.

[10]  N. Hogg,et al.  Identification of p8,14 as a highly abundant heterodimeric calcium binding protein complex of myeloid cells. , 1991, The Journal of biological chemistry.

[11]  C. Figarella,et al.  Identification of 'cystic fibrosis protein' as a complex of two calcium-binding proteins present in human cells of myeloid origin. , 1991, Biochimica et biophysica acta.

[12]  P. Sohnle,et al.  Antimicrobial activity of an abundant calcium-binding protein in the cytoplasm of human neutrophils. , 1991, The Journal of infectious diseases.

[13]  M. Fagerhol,et al.  L1, a major granulocyte protein; isolation of high quantities of its subunits. , 1990, Scandinavian journal of clinical and laboratory investigation.

[14]  E. Lingaas,et al.  Antimicrobial actions of calcium binding leucocyte L1 protein, calprotectin , 1990, The Lancet.

[15]  S. Fleming,et al.  Calgranulin expression and association with the keratinocyte cytoskeleton , 1990, The Journal of pathology.

[16]  S. Fleming,et al.  Calgranulin expression in inflammatory dermatoses , 1989, The Journal of pathology.

[17]  P. Eggleton,et al.  Rapid method for the isolation of neutrophils in high yield without the use of dextran or density gradient polymers. , 1989, Journal of immunological methods.

[18]  P. Brandtzaeg,et al.  Expression of the epithelial L1 antigen as an immunohistochemical marker of squamous cell carcinoma of the lung , 1989, Histopathology.

[19]  M. Fagerhol,et al.  L1, a major granulocyte protein: antigenic properties of its subunits. , 1988, Scandinavian journal of clinical and laboratory investigation.

[20]  C. Hayward,et al.  Expression pattern of two related cystic fibrosis-associated calcium-binding proteins in normal and abnormal tissues. , 1988, Journal of cell science.

[21]  E. Jellum,et al.  The Leucocyte L1 Protein: Identity with the Cystic Fibrosis Antigen and the Calcium‐Binding MRP‐8 and MRP‐14 Macrophage Components , 1988, Scandinavian journal of immunology.

[22]  E. Lagasse,et al.  Cloning and expression of two human genes encoding calcium-binding proteins that are regulated during myeloid differentiation , 1988, Molecular and cellular biology.

[23]  P. Brandtzaeg,et al.  Epithelial distribution of a myelomonocytic antigen L1 in relation to cutaneous malignancies and melanocytic naevi , 1988, The British journal of dermatology.

[24]  R. G. Clerc,et al.  Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis , 1987, Nature.

[25]  P. Brandtzaeg,et al.  Distribution of a formalin-resistant myelomonocytic antigen (L1) in human tissues. II. Normal and aberrant occurrence in various epithelia. , 1987, American journal of clinical pathology.

[26]  P. Brandtzaeg,et al.  Epidermal and dermal distribution of a myelomonocytic antigen (L1) shared by epithelial cells in various inflammatory skin diseases. , 1986, Journal of the American Academy of Dermatology.

[27]  C. Hayward,et al.  The Genetical Society Abstracts of Papers presented at the Two Hundred and Second Meeting of the Society on the 1st, 2nd and 3rd April 1985 at the University of Edinburgh , 1985, Heredity.

[28]  I. Dale,et al.  Purification and partial characterization of a highly immunogenic human leukocyte protein, the L1 antigen. , 1983, European journal of biochemistry.

[29]  G. B. Wilson,et al.  Demonstration of serum protein differences in cystic fibrosis by isoelectric focusing in thin-layer polyacrylamide gels. , 1973, Clinica chimica acta; international journal of clinical chemistry.