Collagen ReI. Res. Vol. 6/1986, pp. 453-454

Nomenclature Recommendations: Bone Proteins and Growth Factors

PETER V. HAUSCHKAt, KENNETH G. MANN2, PAUL A. PRICE3 and JOHND. TERMINE4

I Children's Hospital Medical Center, Boston, Massachusetts, USA. 2 University of Vermont, Burlington, Vermont, USA. 3 University of California, La Jolla, California, USA. 4 National Institutes of Health, Bethesda, Maryland, USA.

The Ad Hoc Committee on Nomenclature and Standards for Bone Proteins and Growth Factors was charged in 1986 by the President and Council of the American Society for Bone and Mineral Research to resolve the ambiguities incurred in evalua­ting data and nomenclature arising from different laboratories. We think that the following suggestions are useful and should be adopted in publishing manuscripts in this area of bone research.

1. Apparent molecular weights for bone proteins and growth factors should be reported, for comparative purposes, as determined on 4-20 % polyacrylamide gra­dient SDS gel electrophoresis run with Laemmli buffers (1970) under reducing condi­tions. Standardization to these easily reproducible, analytical conditions will greatly facilitate comparative examination of such data. For the specific case of conjugate bone proteins (e. g., the proteoglycans), apparent molecular weights should be provided for their respective core proteins.

2. Final assignment of identity for a given bone protein or growth factor should be based on protein sequence analysis. We recommend that the protein or growth factor be described, for comparative purposes, from the IUB single letter code for the first three (3) amino acids of its amino terminal sequence plus its apparent SDS gel molecu­lar weight as determined in recommendation 1 above. When the true molecular weight of the protein is known from complete amino acid sequence data, this should be used preferentially. If the amino terminus of the protein in question is blocked, the amino terminal position in the sequence identification triplet should be represented as X (for unknown) until determined by other means.

3. Other chemical and analytical data are extremely useful. Examples of these are isoelectric point (pI), amino acid composition, oligosaccharide carbohydrate analysis, etc. Such data should always be provided with careful, detailed descriptions and/or citations of the methods used to obtain them.

4. Criteria of purity are always ephemeral; the sensitivity of techniques used for this purpose are continually improved upon. Nevertheless, the best available and most sensitive analytical procedures should always be used whenever appropriate. If only

454 P. V. Hauschka et al.

limited amounts of a protein are available, either (1) silver or colloidal gold staining or (2) radioisotope labeling fluorography of conventional SDS gels would be appropriate methods for this purpose.

5. Experimental procedures used for protein or growth factor isolation should al­ways be described carefully and in detail to assure reproducibility of results from laboratory to laboratory. These include: the ages (and sex, where appropriate) of animals; the anatomical sites, dissection methods, and other conditions used for tissue isolation; chemical extraction methods, cell isolation and culture conditions; immuno­logical procedures, etc.

6. It is recommended that investigators refrain from selecting trivial names for the bone proteins and growth factors which imply biological function or tissue or orgin. These often prove to be incomplete or over-simplified in subsequent studies. If more than one trivial name exists for a known bone protein or growth factor (e. g., osteocal­cin, BGP, bone gla protein), the use ot (me of these in a journal or review article should always be accompanied by footnotes citing (a) the other names commonly used for the protein, and (b) the protein's identification code (if known) as described in recommen­dation, 2 above.

7. It is a convention of science that investigators provide or receive small amounts of materials (proteins, extracts, antibodies, etc.) to facilitate interlaboratory cooperation involved in the identification and verification of experimental results. These courtesies are recognized to be a normal part of interpersonal, scientific interchange.

References

Laemmli, U. K.: Cleavage of structural proteins auring assembly of the head of bacterio­phage T4. Nature 227: 680-685, 1970.

Meeting notice

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