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Nonhaem complexes of FeIII stimulate cell attachment and growth by a mechanism different from that of serum, 2‐oxocarboxylates, and haemproteins
Author(s) -
Kay G. F.,
Ellem K. A. O.
Publication year - 1986
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041260218
Subject(s) - catalase , cell growth , chemistry , redox , cell , function (biology) , biophysics , biochemistry , biology , microbiology and biotechnology , oxidative stress , organic chemistry
Abstract Most cell lines, even those producing their own growth factors, need a serum supplement when growing in several commonly used media. The requirement for serum to sustain attachment and growth in RPMI 1640 and MEM has been found to be met by a range of 2‐oxocarboxylates, by diverse coordination complexes of Felll, and by a variety of haem‐containing proteins including catalase. The latter directly implicates H 2 O 2 in the serum shift‐down effects. H 2 O 2 was found to accumulate in low serum media under normal laboratory lighting conditions to levels that were shown to be sufficient, when added to freshly prepared media, to explain the depressed cell performance. With the exception of some of the nonhaem Felll coordination complexes, substances found to stimulate cell attachment and growth were capable of scavenging H 2 O 2 . This suggests that an important function of serum and the 2‐oxocarboxylates (α‐keto acids) frequently used as “nonessential” medium additives is to remove H 2 O 2 produced photodynamically during the storage and manipulation of media containing a high content of riboflavin. However, the nonhaem Felll complexes with saturated coordination shells, although capable of reducing photodynamic generation of H 2 O 2 to a greater or lesser extent, have their prime effect by an unknown, intriguing mechanism, probably based on a common redox function.