Surfactant protein A

Last updated
surfactant, pulmonary-associated protein A1
Identifiers
SymbolSFTPA1
Alt. symbolsSFTP1
NCBI gene 6435
HGNC 10798
OMIM 178630
RefSeq NM_005411
UniProt Q8IWL2
Other data
Locus Chr. 10 q22.3
surfactant, pulmonary-associated protein A2B
Identifiers
Symbol SFTPA2B
NCBI gene 6436
HGNC 10799
OMIM 178642
RefSeq NM_006926
UniProt Q8IWL1
Other data
Locus Chr. 10 q22.3

Surfactant protein A is an innate immune system collectin. It is water-soluble and has collagen-like domains similar to SP-D. It is part of the innate immune system and is used to opsonize bacterial cells in the alveoli marking them for phagocytosis by alveolar macrophages. SP-A may also play a role in negative feedback limiting the secretion of pulmonary surfactant. SP-A is not required for pulmonary surfactant to function but does confer immune effects to the organism. [1]

Contents

During parturition

The role of surfactant protein A (SP-A) in childbirth is indicated in studies with mice. [2] Mice which gestate for 19 days typically show signs of SP-A in amniotic fluid at around 16 days. If SP-A is injected into the uterus at 15 days, mice typically deliver early. Inversely, an SP-A inhibitor injection causes notable delays in birth.

The presence of surfactant protein A seemed to trigger an inflammatory response in the uterus of the mice, but later studies found an anti-inflammatory response in humans. [3] In fact, the level of SP-A in a human uterus typically decreases during labor.

Immune functions

Research on SP-A has been done mainly in rodents including mice and rats. This research has shown that mice deficient in SP-A are more susceptible to infections from group B Streptoccoal organisms, [4] Pseudomonas aeruginosa, [5] and likely other organisms. The immune functions of SP-A are time, temperature, and concentration dependant. [6]

Location

SP-A is found in the pulmonary surfactant in lungs. SP-A and SP-D are also present in extrapulmonary tissues. [7]

See also

Related Research Articles

Pulmonary alveolus Hollow cavity found in the lungs

A pulmonary alveolus also known as an air sac or air space is one of millions of hollow cup-shaped cavities in the lungs where oxygen is exchanged for carbon dioxide. Alveoli make up the functional tissue of the lungs known as the lung parenchyma, which takes up 90 percent of the total lung volume.

Macrophage Type of white blood cell

Macrophages are a type of white blood cell of the immune system that engulfs and digests anything that does not have, on its surface, proteins that are specific to healthy body cells, including cancer cells, microbes, cellular debris, foreign substances, etc. The process is called phagocytosis, which acts to defend the host against infection and injury.

Pulmonary alveolar proteinosis Medical condition

Pulmonary alveolar proteinosis (PAP) is a rare lung disorder characterized by an abnormal accumulation of surfactant-derived lipoprotein compounds within the alveoli of the lung. The accumulated substances interfere with the normal gas exchange and expansion of the lungs, ultimately leading to difficulty breathing and a predisposition to developing lung infections. The causes of PAP may be grouped into primary, secondary, and congenital causes, although the most common cause is a primary autoimmune condition in an individual.

Pulmonary surfactant

Pulmonary surfactant is a surface-active complex of phospholipids and proteins formed by type II alveolar cells. The proteins and lipids that make up the surfactant have both hydrophilic and hydrophobic regions. By adsorbing to the air-water interface of alveoli, with hydrophilic head groups in the water and the hydrophobic tails facing towards the air, the main lipid component of surfactant, dipalmitoylphosphatidylcholine (DPPC), reduces surface tension.

<i>Pseudomonas aeruginosa</i> Species of bacterium

Pseudomonas aeruginosa is a common encapsulated, Gram-negative, strict aerobic, rod-shaped bacterium that can cause disease in plants and animals, including humans. A species of considerable medical importance, P. aeruginosa is a multidrug resistant pathogen recognized for its ubiquity, its intrinsically advanced antibiotic resistance mechanisms, and its association with serious illnesses – hospital-acquired infections such as ventilator-associated pneumonia and various sepsis syndromes.

<i>Stenotrophomonas maltophilia</i> Species of bacterium

Stenotrophomonas maltophilia is an aerobic, nonfermentative, Gram-negative bacterium. It is an uncommon bacterium and human infection is difficult to treat. Initially classified as Bacterium bookeri, then renamed Pseudomonas maltophilia, S. maltophilia was also grouped in the genus Xanthomonas before eventually becoming the type species of the genus Stenotrophomonas in 1993.

Collectins (collagen-containing C-type lectins) are a part of the innate immune system. They form a family of collagenous Ca2+-dependent defense lectins, which are found in animals. Collectins are soluble pattern recognition receptors (PRRs). Their function is to bind to oligosaccharide structure or lipids that are on the surface of microorganisms. Like other PRRs they bind pathogen-associated molecular patterns (PAMPs) and danger-associated molecular patterns (DAMPs) of oligosaccharide origin. Binding of collectins to microorganisms may trigger elimination of microorganisms by aggregation, complement activation, opsonization, activation of phagocytosis, or inhibition of microbial growth. Other functions of collectins are modulation of inflammatory, allergic responses, adaptive immune system and clearance of apoptotic cells.

Surfactant protein D

Surfactant protein D, also known as SP-D, is a lung surfactant protein part of the collagenous family of proteins called collectin. In humans, SP-D is encoded by the SFTPD gene and is part of the innate immune system. Each SP-D subunit is composed of an N-terminal domain, a collagenous region, a nucleating neck region, and a C-terminal lectin domain. Three of these subunits assemble to form a homotrimer, which further assemble into a tetrameric complex.

Surfactant protein B

Surfactant protein B is an essential lipid-associated protein found in pulmonary surfactant. Without it, the lung would not be able to inflate after a deep breath out. It rearranges lipid molecules in the fluid lining the lung so that tiny air sacs in the lung, called alveoli, can more easily inflate.

Surfactant protein C

Surfactant protein C (SP-C), is one of the pulmonary surfactant proteins. In humans this is encoded by the SFTPC gene.

Ecthyma gangrenosum Medical condition

Ecthyma gangrenosum is a type of skin lesion characterized by vesicles or blisters which rapidly evolve into pustules and necrotic ulcers with undermined tender erythematous border. "Ecthyma" means a pus forming infection of the skin with an ulcer, "gangrenosum" refers to the accompanying gangrene or necrosis. It is classically associated with Pseudomonas aeruginosa bacteremia, but it is not pathognomonic. Pseudomonas aeruginosa is a gram negative, aerobic bacillus.

DMBT1

Deleted in malignant brain tumors 1 protein is a protein that in humans is encoded by the DMBT1 gene.

Surfactant protein A1

Surfactant protein A1(SP-A1), also known as Pulmonary surfactant-associated protein A1(PSP-A) is a protein that in humans is encoded by the SFTPA1 gene.

Peptidoglycan recognition protein 2

Peptidoglycan recognition protein 2(PGLYRP2) is an enzyme, N-acetylmuramoyl-L-alanine amidase (NAMLAA), that hydrolyzes bacterial cell wall peptidoglycan and is encoded by the PGLYRP2 gene.

Peptidoglycan recognition protein 1

Peptidoglycan recognition protein 1, PGLYRP1, also known as TAG7, is an antibacterial and pro-inflammatory innate immunity protein that in humans is encoded by the PGLYRP1 gene.

Surfactant protein A2

Surfactant protein A2(SP-A2), also known as Pulmonary surfactant-associated protein A2(PSP-A2) is a protein that in humans is encoded by the SFTPA2 gene.

Surfactant metabolism dysfunction is a condition where pulmonary surfactant is insufficient for adequate respiration. Surface tension at the liquid-air interphase in the alveoli makes the air sacs prone to collapsing post expiration. This is due to the fact that water molecules in the liquid-air surface of alveoli are more attracted to one another than they are to molecules in the air. For sphere-like structures like alveoli, water molecules line the inner walls of the air sacs and stick tightly together through hydrogen bonds. These intermolecular forces put great restraint on the inner walls of the air sac, tighten the surface all together, and unyielding to stretch for inhalation. Thus, without something to alleviate this surface tension, alveoli can collapse and cannot be filled up again. Surfactant is essential mixture that is released into the air-facing surface of inner walls of air sacs to lessen the strength of surface tension. This mixture inserts itself among water molecules and breaks up hydrogen bonds that hold the tension. Multiple lung diseases, like ISD or RDS, in newborns and late-onsets cases have been linked to dysfunction of surfactant metabolism.

Pulmonary surfactant protein D

In molecular biology, Pulmonary surfactant protein D (SP-D) is a protein domain predominantly found in lung surfactant. This protein plays a special role; its primary task is to act as a defence protein against any pathogens that may invade the lung. It also plays a role in lubricating the lung and preventing it from collapse. It has an interesting structure as it forms a triple-helical parallel coiled coil, helps the protein to fold into a trimer.

The lung microbiota, is the pulmonary microbial community consisting of a complex variety of microorganisms found in the lower respiratory tract particularly on the mucous layer and the epithelial surfaces. These microorganisms include bacteria, fungi, viruses and bacteriophages. The bacterial part of the microbiota has been more closely studied. It consists of a core of nine genera: Prevotella, Sphingomonas, Pseudomonas, Acinetobacter, Fusobacterium, Megasphaera, Veillonella, Staphylococcus, and Streptococcus. They are aerobes as well as anaerobes and aerotolerant bacteria. The microbial communities are highly variable in particular individuals and compose of about 140 distinct families. The bronchial tree for instance contains a mean of 2000 bacterial genomes per cm2 surface. The harmful or potentially harmful bacteria are also detected routinely in respiratory specimens. The most significant are Moraxella catarrhalis, Haemophilus influenzae, and Streptococcus pneumoniae. They are known to cause respiratory disorders under particular conditions namely if the human immune system is impaired. The mechanism by which they persist in the lower airways in healthy individuals is unknown.

Pneumocystis murina is a species of fungus, first isolated from laboratory mice, hence its name.

References

  1. Boron W, Boulpaep E (2012). Medical Physiology (2nd ed.). Philadelphia: Elsevier.
  2. Condon JC, Jeyasuria P, Faust JM, Mendelson CR (April 2004). "Surfactant protein secreted by the maturing mouse fetal lung acts as a hormone that signals the initiation of parturition". Proceedings of the National Academy of Sciences of the United States of America. 101 (14): 4978–83. Bibcode:2004PNAS..101.4978C. doi: 10.1073/pnas.0401124101 . JSTOR   3371804. PMC   387359 . PMID   15044702.
  3. Lee DC, Romero R, Kim CJ, Chaiworapongsa T, Tarca AL, Lee J, Suh YL, Mazaki-Tovi S, Vaisbuch E, Mittal P, Draghici S, Erez O, Kusanovic JP, Hassan SS, Kim JS (June 2010). "Surfactant protein-A as an anti-inflammatory component in the amnion: implications for human pregnancy". Journal of Immunology. 184 (11): 6479–91. doi:10.4049/jimmunol.0903867. PMC   3103775 . PMID   20439915.
  4. LeVine AM, Bruno MD, Huelsman KM, Ross GF, Whitsett JA, Korfhagen TR (May 1997). "Surfactant protein A-deficient mice are susceptible to group B streptococcal infection". Journal of Immunology. 158 (9): 4336–40. PMID   9126996.
  5. LeVine AM, Kurak KE, Bruno MD, Stark JM, Whitsett JA, Korfhagen TR (October 1998). "Surfactant protein-A-deficient mice are susceptible to Pseudomonas aeruginosa infection". American Journal of Respiratory Cell and Molecular Biology. 19 (4): 700–8. doi:10.1165/ajrcmb.19.4.3254. PMID   9761768.
  6. van Iwaarden F, Welmers B, Verhoef J, Haagsman HP, van Golde LM (January 1990). "Pulmonary surfactant protein A enhances the host-defense mechanism of rat alveolar macrophages". American Journal of Respiratory Cell and Molecular Biology. 2 (1): 91–8. doi:10.1165/ajrcmb/2.1.91. PMID   2306370.
  7. Haagsman HP, Diemel RV (May 2001). "Surfactant-associated proteins: functions and structural variation". Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology. 129 (1): 91–108. doi:10.1016/s1095-6433(01)00308-7. PMID   11369536.