Augmentation of the antibody response by antigen-specific glycosylation-enhancing factor

M. Iwata, Y. Fukutomi, T. Hashimoto, Y. Sato, H. Sato, K. Ishizaka

Research output: Contribution to journalArticle

Abstract

BDF1 mice were immunized with a protein antigen, such as ovalbumin (OA) or keyhole limpet hemocyanin (KLH), absorbed to aluminium hydroxide gel, and their spleen cells were stimulated by homologous antigen for the formation of glycosylation-enhancing factor (GEF). It was found that GEF obtained from OA-primed spleen cells had affinity for OA, whereas those derived from KLH-primed spleen cells had affinity for KLH. Nonspecific GEF, which was obtained by stimulation of normal spleen cells with pertussis toxin, failed to bind OA or KLH. Both antigen-specific GEF and nonspecific GEF are inactivated by phenylmethylsulfonyl fluoride, but not by N-α-p-tosyl-L-lysyl-chloromethyl ketone. Both factors can be partially purified by binding to p-aminobenzamidine agarose and elution with benzamidine. These findings suggest that not only nonspecific GEF but also antigen-specific GEF are serine protease(s). The antigen-specific GEF consisted of two m.w. species, of 65 to 85 kilodaltons (Kd) and 40 to 55 Kd, whereas nonspecific GEF consisted of 50 to 70 Kd and 20 to 30 Kd molecules. The OA-specific GEF augmented the in vitro secondary indirect PFC response of DNP-OA-primed cells to the homologous antigen, but failed to affect the PFC response of DNP-KLH-primed cells to DNP-KLH. Similarly, KLH-specific GEF enhanced the response of DNP-KLH-primed cells but not the response of DNP-OA-primed cells. However, OA-specific GEF failed to replace the requirement for antigen-primed helper T cells. Antigen-specific GEF bound to alloantibodies reactive to the products of the I region of the major histocompatibility complex. The results collectively suggest that antigen-specific GEF is identical to antigen-specific augmenting factors described by other investigators.

Original languageEnglish (US)
Pages (from-to)2561-2567
Number of pages7
JournalJournal of Immunology
Volume138
Issue number8
StatePublished - 1987
Externally publishedYes

Fingerprint

Antibody Formation
Antigens
Ovalbumin
Spleen
immunoglobulin-binding factors
Phenylmethylsulfonyl Fluoride
Aluminum Hydroxide
Isoantibodies
keyhole-limpet hemocyanin
Pertussis Toxin
Serine Proteases
Helper-Inducer T-Lymphocytes
Major Histocompatibility Complex
Ketones
Sepharose
Research Personnel

ASJC Scopus subject areas

  • Immunology

Cite this

Iwata, M., Fukutomi, Y., Hashimoto, T., Sato, Y., Sato, H., & Ishizaka, K. (1987). Augmentation of the antibody response by antigen-specific glycosylation-enhancing factor. Journal of Immunology, 138(8), 2561-2567.

Augmentation of the antibody response by antigen-specific glycosylation-enhancing factor. / Iwata, M.; Fukutomi, Y.; Hashimoto, T.; Sato, Y.; Sato, H.; Ishizaka, K.

In: Journal of Immunology, Vol. 138, No. 8, 1987, p. 2561-2567.

Research output: Contribution to journalArticle

Iwata, M, Fukutomi, Y, Hashimoto, T, Sato, Y, Sato, H & Ishizaka, K 1987, 'Augmentation of the antibody response by antigen-specific glycosylation-enhancing factor', Journal of Immunology, vol. 138, no. 8, pp. 2561-2567.
Iwata M, Fukutomi Y, Hashimoto T, Sato Y, Sato H, Ishizaka K. Augmentation of the antibody response by antigen-specific glycosylation-enhancing factor. Journal of Immunology. 1987;138(8):2561-2567.
Iwata, M. ; Fukutomi, Y. ; Hashimoto, T. ; Sato, Y. ; Sato, H. ; Ishizaka, K. / Augmentation of the antibody response by antigen-specific glycosylation-enhancing factor. In: Journal of Immunology. 1987 ; Vol. 138, No. 8. pp. 2561-2567.
@article{3b315c8e9ba840448dd36f1eb29cce86,
title = "Augmentation of the antibody response by antigen-specific glycosylation-enhancing factor",
abstract = "BDF1 mice were immunized with a protein antigen, such as ovalbumin (OA) or keyhole limpet hemocyanin (KLH), absorbed to aluminium hydroxide gel, and their spleen cells were stimulated by homologous antigen for the formation of glycosylation-enhancing factor (GEF). It was found that GEF obtained from OA-primed spleen cells had affinity for OA, whereas those derived from KLH-primed spleen cells had affinity for KLH. Nonspecific GEF, which was obtained by stimulation of normal spleen cells with pertussis toxin, failed to bind OA or KLH. Both antigen-specific GEF and nonspecific GEF are inactivated by phenylmethylsulfonyl fluoride, but not by N-α-p-tosyl-L-lysyl-chloromethyl ketone. Both factors can be partially purified by binding to p-aminobenzamidine agarose and elution with benzamidine. These findings suggest that not only nonspecific GEF but also antigen-specific GEF are serine protease(s). The antigen-specific GEF consisted of two m.w. species, of 65 to 85 kilodaltons (Kd) and 40 to 55 Kd, whereas nonspecific GEF consisted of 50 to 70 Kd and 20 to 30 Kd molecules. The OA-specific GEF augmented the in vitro secondary indirect PFC response of DNP-OA-primed cells to the homologous antigen, but failed to affect the PFC response of DNP-KLH-primed cells to DNP-KLH. Similarly, KLH-specific GEF enhanced the response of DNP-KLH-primed cells but not the response of DNP-OA-primed cells. However, OA-specific GEF failed to replace the requirement for antigen-primed helper T cells. Antigen-specific GEF bound to alloantibodies reactive to the products of the I region of the major histocompatibility complex. The results collectively suggest that antigen-specific GEF is identical to antigen-specific augmenting factors described by other investigators.",
author = "M. Iwata and Y. Fukutomi and T. Hashimoto and Y. Sato and H. Sato and K. Ishizaka",
year = "1987",
language = "English (US)",
volume = "138",
pages = "2561--2567",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "8",

}

TY - JOUR

T1 - Augmentation of the antibody response by antigen-specific glycosylation-enhancing factor

AU - Iwata, M.

AU - Fukutomi, Y.

AU - Hashimoto, T.

AU - Sato, Y.

AU - Sato, H.

AU - Ishizaka, K.

PY - 1987

Y1 - 1987

N2 - BDF1 mice were immunized with a protein antigen, such as ovalbumin (OA) or keyhole limpet hemocyanin (KLH), absorbed to aluminium hydroxide gel, and their spleen cells were stimulated by homologous antigen for the formation of glycosylation-enhancing factor (GEF). It was found that GEF obtained from OA-primed spleen cells had affinity for OA, whereas those derived from KLH-primed spleen cells had affinity for KLH. Nonspecific GEF, which was obtained by stimulation of normal spleen cells with pertussis toxin, failed to bind OA or KLH. Both antigen-specific GEF and nonspecific GEF are inactivated by phenylmethylsulfonyl fluoride, but not by N-α-p-tosyl-L-lysyl-chloromethyl ketone. Both factors can be partially purified by binding to p-aminobenzamidine agarose and elution with benzamidine. These findings suggest that not only nonspecific GEF but also antigen-specific GEF are serine protease(s). The antigen-specific GEF consisted of two m.w. species, of 65 to 85 kilodaltons (Kd) and 40 to 55 Kd, whereas nonspecific GEF consisted of 50 to 70 Kd and 20 to 30 Kd molecules. The OA-specific GEF augmented the in vitro secondary indirect PFC response of DNP-OA-primed cells to the homologous antigen, but failed to affect the PFC response of DNP-KLH-primed cells to DNP-KLH. Similarly, KLH-specific GEF enhanced the response of DNP-KLH-primed cells but not the response of DNP-OA-primed cells. However, OA-specific GEF failed to replace the requirement for antigen-primed helper T cells. Antigen-specific GEF bound to alloantibodies reactive to the products of the I region of the major histocompatibility complex. The results collectively suggest that antigen-specific GEF is identical to antigen-specific augmenting factors described by other investigators.

AB - BDF1 mice were immunized with a protein antigen, such as ovalbumin (OA) or keyhole limpet hemocyanin (KLH), absorbed to aluminium hydroxide gel, and their spleen cells were stimulated by homologous antigen for the formation of glycosylation-enhancing factor (GEF). It was found that GEF obtained from OA-primed spleen cells had affinity for OA, whereas those derived from KLH-primed spleen cells had affinity for KLH. Nonspecific GEF, which was obtained by stimulation of normal spleen cells with pertussis toxin, failed to bind OA or KLH. Both antigen-specific GEF and nonspecific GEF are inactivated by phenylmethylsulfonyl fluoride, but not by N-α-p-tosyl-L-lysyl-chloromethyl ketone. Both factors can be partially purified by binding to p-aminobenzamidine agarose and elution with benzamidine. These findings suggest that not only nonspecific GEF but also antigen-specific GEF are serine protease(s). The antigen-specific GEF consisted of two m.w. species, of 65 to 85 kilodaltons (Kd) and 40 to 55 Kd, whereas nonspecific GEF consisted of 50 to 70 Kd and 20 to 30 Kd molecules. The OA-specific GEF augmented the in vitro secondary indirect PFC response of DNP-OA-primed cells to the homologous antigen, but failed to affect the PFC response of DNP-KLH-primed cells to DNP-KLH. Similarly, KLH-specific GEF enhanced the response of DNP-KLH-primed cells but not the response of DNP-OA-primed cells. However, OA-specific GEF failed to replace the requirement for antigen-primed helper T cells. Antigen-specific GEF bound to alloantibodies reactive to the products of the I region of the major histocompatibility complex. The results collectively suggest that antigen-specific GEF is identical to antigen-specific augmenting factors described by other investigators.

UR - http://www.scopus.com/inward/record.url?scp=0023114946&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023114946&partnerID=8YFLogxK

M3 - Article

C2 - 3494077

AN - SCOPUS:0023114946

VL - 138

SP - 2561

EP - 2567

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 8

ER -