Immunology Today, vol. 8, No. 4, 1987
-rostrum
II1,1 . . . . . . .
glucose starvation or heat shock many proteins fail to assemble or fold correctly 3°. The speculation that BiP interacts with a hydrophobic portion of the protein or an unpaired sulfhydryl group which is unavailable after protein folding and subunit assembly might best explain the ability of BiP to associate post-translationally with various non-immunoglobulin proteins. In conclusion, BiP appears to play a role in the normal transport of Ig molecules by ensuring that only completely assembled heavy chains are secreted or inserted in the surface membrane, thus helping to establish the observed phenotypes for pre-B (cytoplasmic I~), B (surface Ig +, secretion-) and plasma cells. In this way, it may greatly aid the efficient functioning of the immune system at the various stages of B-cell differentiation. Further, it seems likely that the inability of BiP to associate with the heavy chain disease proteins (CH1-) allows these mutant HC to be secreted without LC. In this same vein, BiP may play a role in diminishing the ability of most HC-only iymphomas CH1 + to survive, thus contributing to the phenotype of observed lymphomas and myelomas. This work has been supported by USPHSGrants A 16673, CA 13148 and AI 23526-01. References
1 Morrison, S.L. and Scharff, M.D. (1975)J. Immunol. 114, 655-659 2 Haas,I. and Wabl, M. (1983) Nature (London) 306, 387-389 3 Bole, D., Hendershot, L. and Kearney,J.F.(1984) Fed. Proc. 43, 1406-1417 4 Bole, D., Hendershot, L. and Kearney,J.F.(1986) J. CellBiol. 102, 1558-1566 5 Tartakoff, A. and Vassalli, P. (1979) J. CellBiol. 83, 284-299 6 Baxbaum,J. and Scharff, M.D. (1973)J. Exp. Med. 138, 278-288 7 Blobel, G. and Dobberstein, B. (1975)J. CellBiol. 67, 835-8_57
8 Bergman, L.W. and KuehloW.M. (1978) Biochemistry 17, 5174-5180 9 Hubbard, S.C. and Ivatt, R.J.(1981)Annu. Rev. Biochem. 50, 555-583 10 Palade, G. (1975)Science 189, 347-358 11 Fitting, T. and Kabat, D. (1982) J. BioL Chem. 257, 14011-14017 12 Lodish, H.F., Kong, N., Snider, M. and Strous, G.J.A.M. (1983) Nature (London) 304, 80-83 13 McCune and Fu, S.-M. (1981)J. ImmunoL 127, 2609-2611 14 Franklin, E.C. and FrangioneoB. (1975)in Contemporary Topics in .A/.olecularImmunology (Vol. 126) (Inman, F.P.and Mandy, W., eds), p. 89, Plenum, New York 15 Burrows, P., Lejeune, M. and Kearney, F.J.(1979)Nature (London) 280, 838-841 16 Thorens, B., Schulz, M.-F. and Vassalli, P. (1985)EMBOJ. 4, 361-368 17 Warner, N. (1974)Adv. ImmunoL 19, 67-216 18 Sidman, C. (1981) Cell 23, 379-389 19 Seligmann, M., Mihaesco, E., Preud'homme, J.-L etaL (1979) ImmunoL Rev. 48, 145-167 20 Morrison, S.L (1978)Eur. J. ImmunoL 8, 194-199 21 Dackowski, W. and Morrison, S.L. (1981)Proc. NatlAcad. Sci. USA 78, 7091-7095 22 Hendershot, L., Bole, D. and Kearney, J.F.J. CellBioL (in press) 23 Edmundson, A.B., Ely, K.R., Abola, E.E.etal. (1975) Biochemistry 14, 3953-3961 24 Jeske, D.J. and Capra, J.D. (1984) in Fundamental Immunology (Paul, W.E., ed.), pp. 131-165, Raven Press, New York 25 Abel, C.A. and Gray, H.M. (1968)Biochemistry7, 2682-2688 26 Azar, H.A. (1973)in The Myeloma Cell (Azar, H.A. and Potter, M., eds), pp. 86-152, Harper and Row, New York 27 Weitzman, S., Margulies, D.H. and Scharff, M.D. (1976) Ann. Int. Med. 85, 110-115 28 Osserman, E.F.and Taratsubi, K. (1963) Medicine 42, 357-384 29 Gething, M.-J., McCammon, K. and Sambrook, J. (1986) Cell 46, 939-950 ~A,i~r.'~ IVIUI IIU#
S
-J.~..,l D . , ~ l l , . ~ m U D D IINOr'% . a l l U I - ~ 1 1 ICII I I , I 1. 1~ . ~ 1. ~ I ~ O U /
I"..11 lit= %-I~11 ~ U ,
"tt~'l L~ I
"~rt.~ .~UU
Erratum Characterizationof humanleukocytediflerentiationantigens StephenShaw(1987)Imrnunol.Today8, I-3 A portion of the table in Dr Shaw'sarticlewhich listedthe CD antigensand their distributioncontainederrors introducedwhen correctionswere made late in the journal'sproduction.The correctversior is printed below. We apologisefor this lapse. CD38 CD39 CDw40 CDw41 CDw42 CD43 CD44 CD45 CD45R
45 80 50 95 65-85 220,205,190, 180 220, 205
restrictedmultiplelineages Bcells,macrophages,vessels Bcells,carcinomas,ClRC platelets platelets T cells,granulocytes°red cells,brain T cells,ph'e-B,brain,granulocytes leucoc/tes Bcells,T subset,granulocytes,monocytes
T10 gpllb/llla gplb T200, LCA restrictedT200 2H4 etc.
-rostrum
II1,1 . . . . . . .
glucose starvation or heat shock many proteins fail to assemble or fold correctly 3°. The speculation that BiP interacts with a hydrophobic portion of the protein or an unpaired sulfhydryl group which is unavailable after protein folding and subunit assembly might best explain the ability of BiP to associate post-translationally with various non-immunoglobulin proteins. In conclusion, BiP appears to play a role in the normal transport of Ig molecules by ensuring that only completely assembled heavy chains are secreted or inserted in the surface membrane, thus helping to establish the observed phenotypes for pre-B (cytoplasmic I~), B (surface Ig +, secretion-) and plasma cells. In this way, it may greatly aid the efficient functioning of the immune system at the various stages of B-cell differentiation. Further, it seems likely that the inability of BiP to associate with the heavy chain disease proteins (CH1-) allows these mutant HC to be secreted without LC. In this same vein, BiP may play a role in diminishing the ability of most HC-only iymphomas CH1 + to survive, thus contributing to the phenotype of observed lymphomas and myelomas. This work has been supported by USPHSGrants A 16673, CA 13148 and AI 23526-01. References
1 Morrison, S.L. and Scharff, M.D. (1975)J. Immunol. 114, 655-659 2 Haas,I. and Wabl, M. (1983) Nature (London) 306, 387-389 3 Bole, D., Hendershot, L. and Kearney,J.F.(1984) Fed. Proc. 43, 1406-1417 4 Bole, D., Hendershot, L. and Kearney,J.F.(1986) J. CellBiol. 102, 1558-1566 5 Tartakoff, A. and Vassalli, P. (1979) J. CellBiol. 83, 284-299 6 Baxbaum,J. and Scharff, M.D. (1973)J. Exp. Med. 138, 278-288 7 Blobel, G. and Dobberstein, B. (1975)J. CellBiol. 67, 835-8_57
8 Bergman, L.W. and KuehloW.M. (1978) Biochemistry 17, 5174-5180 9 Hubbard, S.C. and Ivatt, R.J.(1981)Annu. Rev. Biochem. 50, 555-583 10 Palade, G. (1975)Science 189, 347-358 11 Fitting, T. and Kabat, D. (1982) J. BioL Chem. 257, 14011-14017 12 Lodish, H.F., Kong, N., Snider, M. and Strous, G.J.A.M. (1983) Nature (London) 304, 80-83 13 McCune and Fu, S.-M. (1981)J. ImmunoL 127, 2609-2611 14 Franklin, E.C. and FrangioneoB. (1975)in Contemporary Topics in .A/.olecularImmunology (Vol. 126) (Inman, F.P.and Mandy, W., eds), p. 89, Plenum, New York 15 Burrows, P., Lejeune, M. and Kearney, F.J.(1979)Nature (London) 280, 838-841 16 Thorens, B., Schulz, M.-F. and Vassalli, P. (1985)EMBOJ. 4, 361-368 17 Warner, N. (1974)Adv. ImmunoL 19, 67-216 18 Sidman, C. (1981) Cell 23, 379-389 19 Seligmann, M., Mihaesco, E., Preud'homme, J.-L etaL (1979) ImmunoL Rev. 48, 145-167 20 Morrison, S.L (1978)Eur. J. ImmunoL 8, 194-199 21 Dackowski, W. and Morrison, S.L. (1981)Proc. NatlAcad. Sci. USA 78, 7091-7095 22 Hendershot, L., Bole, D. and Kearney, J.F.J. CellBioL (in press) 23 Edmundson, A.B., Ely, K.R., Abola, E.E.etal. (1975) Biochemistry 14, 3953-3961 24 Jeske, D.J. and Capra, J.D. (1984) in Fundamental Immunology (Paul, W.E., ed.), pp. 131-165, Raven Press, New York 25 Abel, C.A. and Gray, H.M. (1968)Biochemistry7, 2682-2688 26 Azar, H.A. (1973)in The Myeloma Cell (Azar, H.A. and Potter, M., eds), pp. 86-152, Harper and Row, New York 27 Weitzman, S., Margulies, D.H. and Scharff, M.D. (1976) Ann. Int. Med. 85, 110-115 28 Osserman, E.F.and Taratsubi, K. (1963) Medicine 42, 357-384 29 Gething, M.-J., McCammon, K. and Sambrook, J. (1986) Cell 46, 939-950 ~A,i~r.'~ IVIUI IIU#
S
-J.~..,l D . , ~ l l , . ~ m U D D IINOr'% . a l l U I - ~ 1 1 ICII I I , I 1. 1~ . ~ 1. ~ I ~ O U /
I"..11 lit= %-I~11 ~ U ,
"tt~'l L~ I
"~rt.~ .~UU
Erratum Characterizationof humanleukocytediflerentiationantigens StephenShaw(1987)Imrnunol.Today8, I-3 A portion of the table in Dr Shaw'sarticlewhich listedthe CD antigensand their distributioncontainederrors introducedwhen correctionswere made late in the journal'sproduction.The correctversior is printed below. We apologisefor this lapse. CD38 CD39 CDw40 CDw41 CDw42 CD43 CD44 CD45 CD45R
45 80 50 95 65-85 220,205,190, 180 220, 205
restrictedmultiplelineages Bcells,macrophages,vessels Bcells,carcinomas,ClRC platelets platelets T cells,granulocytes°red cells,brain T cells,ph'e-B,brain,granulocytes leucoc/tes Bcells,T subset,granulocytes,monocytes
T10 gpllb/llla gplb T200, LCA restrictedT200 2H4 etc.
