RT Book, Section
A1 Kipps, Thomas J.
A2 Kaushansky, Kenneth
A2 Prchal, Josef T.
A2 Burns, Linda J.
A2 Lichtman, Marshall A.
A2 Levi, Marcel
A2 Linch, David C.
SR Print(0)
ID 1180446176
T1 Functions of B Lymphocytes and Plasma Cells in Immunoglobulin Production
T2 Williams Hematology, 10e
YR 2021
FD 2021
PB McGraw-Hill Education
PP New York, NY
SN 9781260464122
LK accessmedicine.mhmedical.com/content.aspx?aid=1180446176
RD 2024/04/20
AB SUMMARYMuch  of  our  immune  defense  against  invading  organisms  is  predicated  upon  the  tremendous  diversity  of  immunoglobulin  (Ig)  molecules.  Igs  are  glycoproteins  produced  by  B  lymphocytes  and  plasma  cells.  These  molecules  can  be  considered  receptors  because  the  primary  function  of  the  Ig  molecule  is  to  bind  antigen.  A  single  person  can  synthesize  10–100  million  different  Ig  molecules,  each  having  a  distinct  antigen-binding  specificity.  The  great  diversity  in  this  so-called  humoral  immune  system  allows  us  to  generate  antibodies  specific  for  a  variety  of  substances,  including  synthetic  molecules  not  naturally  present  in  our  environment.  Despite  the  diversity  in  the  specificities  of  antibody  molecules,  the  binding  of  antibody  to  antigen  initiates  a  limited  series  of  biologically  important  effector  functions,  such  as  complement  activation  or  adherence  of  the  immune  complex  to  receptors  on  leukocytes.  The  eventual  outcome  is  the  clearance  and  degradation  of  the  foreign  substance.  This  chapter  describes  the  structure  of  Igs  and  outlines  the  mechanisms  by  which  B  cells  produce  molecules  of  such  tremendous  diversity  with  defined  effector  functions.