Linked Life Data

11948618

Source:http://linkedlifedata.com/resource/pubmed/id/11948618

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-4-11
pubmed:abstractText
Immune systems are, increasingly, being studied from comparative perspectives. The analysis of the immune-defense systems of invertebrates, such as fruit flies and earthworms, is an important part of this effort. These systems are innate, natural non-specific, non-anticipatory and non-clonal. This is in contrast to the macrophage T and B systems that characterize vertebrate adaptive immunity whose properties can be categorized as adaptive, induced, specific, anticipatory, and clonal. In this review, we will focus on the earthworm system. Earthworms, like other complex invertebrates, possess several leukocyte types and synthesize and secrete a variety of immunoprotective molecules. The system as a whole effects phagocytosis, encapsulation, agglutination, opsonization, clotting and lysis of foreign components. At least two major leukocytes, small coelomocytes, and large coelomocytes mediate lytic reactions against several targets. Destruction of tumor cells in vitro shows that phagocytosis and natural killer cell responses are distinct properties of coelomocytes. A third type, the chlorogogen cell, synthesizes and sheds effector lytic molecules. Among the lytic molecules, three have been identified and sequenced (fetidins, CCF-1, lysenin) and another has been discovered (eiseniapore), while three other molecules, H(1) H(2) H(3), share agglutinating and lysing functions. In contrast to these, Lumbricin I is the only known molecule of the earthworm system that is antimicrobial but non-lytic. Altogether the cellular and humoral components of the earthworm system function to distinguish between self and not self, dispose of internal (cancer?), damaged components and external antigens (microbes). The evolutionary context of the earthworm innate immune system is discussed at the end of this article.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0265-9247
pubmed:author
pubmed:copyrightInfo
Copyright 2002 Wiley Periodicals, Inc.
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
319-33
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:11948618-Amino Acid Sequence, pubmed-meshheading:11948618-Animals, pubmed-meshheading:11948618-Cytotoxins, pubmed-meshheading:11948618-Hemolysin Proteins, pubmed-meshheading:11948618-Immune System, pubmed-meshheading:11948618-Immunity, pubmed-meshheading:11948618-Invertebrates, pubmed-meshheading:11948618-Killer Cells, Natural, pubmed-meshheading:11948618-Lectins, pubmed-meshheading:11948618-Models, Immunological, pubmed-meshheading:11948618-Molecular Sequence Data, pubmed-meshheading:11948618-Phagocytosis, pubmed-meshheading:11948618-Proteins, pubmed-meshheading:11948618-Sequence Alignment, pubmed-meshheading:11948618-Sequence Homology, Amino Acid, pubmed-meshheading:11948618-Serine Endopeptidases, pubmed-meshheading:11948618-Toxins, Biological, pubmed-meshheading:11948618-Vertebrates
pubmed:year
2002
pubmed:articleTitle
Digging for innate immunity since Darwin and Metchnikoff.
pubmed:affiliation
Laboratory of Comparative Immunology, UCLA, Los Angeles 90095-1763, USA. cooper@mednet.ucla.edu
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't