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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Isomerism in Complexes
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In this lesson, we delve into the role of ring conformation and its stability, which determines the spatial arrangement and, consequently, the molecular symmetry and stereoisomerism of cyclic compounds. 1,2-Dimethylcyclohexane is used as a case study to evaluate the possible number of stereoisomers. Here, given the multiple (n = 2) chiral centers, there are 2n = 4 possible configurations that lack a plane of symmetry, as the ring skeleton exists in a non-planar chair conformation. In addition,...
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Depending upon the different spatial orientation of the substituents, the disubstituted cycloalkanes exhibit two types of stereoisomers. The cis isomers have the substituents on the same side of the ring, whereas the trans isomers have the substituents on the opposite sides. These stereoisomers exhibit different physical properties and cannot be interconverted without breaking the carbon-carbon bonds.
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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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CL-11 circulates in serum as functionally distinct isoforms.

Adrian Sutta1,2, Nelia Nina Leemans1, Michael Ploug3,4

  • 1Laboratory of Molecular Medicine, Department of Clinical Immunology, Copenhagen University Hospital: Rigshospital, Copenhagen, Denmark.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|March 11, 2024
PubMed
Summary
This summary is machine-generated.

Collectin-11 (CL-11) isoforms A and D exhibit distinct biological functions. CL-11D shows reduced interaction with collectin-10 (CL-10) and lower ligand binding, potentially limiting its complement activation role.

Keywords:
CL-10CL-11MASPcollectincomplement systemlectin pathway

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Immunohistochemical Analysis in the Rat Central Nervous System and Peripheral Lymph Node Tissue Sections
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Area of Science:

  • Immunology
  • Molecular Biology
  • Complement System

Background:

  • Collectin-11 (CL-11) is a pattern recognition molecule in the lectin complement pathway.
  • Alternative splicing of the COLEC11 gene produces serum isoforms A and D, differing in collagen-like region length.
  • These isoforms' biological differences and impact on complement activation are not fully understood.

Purpose of the Study:

  • To elucidate the biological differences between CL-11 isoforms A and D.
  • To investigate their interactions with collectin-10 (CL-10) and MASPs.
  • To assess their potential roles in complement cascade activation.

Main Methods:

  • Production of recombinant CL-11 isoforms (A and D) and CL-10/11 complexes.
  • Analysis of CL-10/11 heterocomplex formation and stability.
  • Immunoprecipitation of serum CL-11 followed by mass spectrometry.
  • Assessment of MASP and ligand binding capabilities of CL-11 isoforms.

Main Results:

  • Both CL-11 isoforms associated with CL-10, with CL-11D showing reduced binding.
  • CL-10/11 heterocomplexes formed, exhibiting greater stability than homotrimers.
  • Native CL-11 circulates as CL-10/11 heterocomplexes with MASP-1 and MASP-3.
  • CL-11D bound MASPs but had reduced ligand binding compared to CL-11A.
  • CL-11D demonstrated reduced oligomerization and heterocomplex formation.

Conclusions:

  • CL-11D's shorter collagen region does not prevent MASP binding but reduces ligand interaction and heterocomplex formation.
  • CL-11D may possess a limited complement activation potential compared to the full-length CL-11A isoform.
  • These findings highlight functional distinctions between CL-11 isoforms in complement regulation.