Lactose-binding lectin from Vatairea macrocarpa seeds induces in vivo angiogenesis via VEGF and TNF-ɑ expression and modulates in vitro doxorubicin-induced genotoxicity

L-14 is a divalent, lactosamine-binding lectin expressed in many vertebrate tissues. In the rat nervous system, L-14 expression has been observed previously in restricted neuronal subsets within the dorsal root ganglia and spinal cord. In this study we report that L-14 is expressed by nonneuronal cells in the rat olfactory nerve. We demonstrate that L-14 binds and co-localizes with two ligands in the rat olfactory system: a beta-lactosamine-containing glycolipid, and a putative member of the laminin family. The former is expressed on the surfaces of nascent olfactory axons originating from neuron cell bodies in the olfactory epithelium. The latter is present in the extracellular matrix of the axonal path leading to synaptic targets in the olfactory bulb. In vitro, we find that recombinant L-14 promotes primary olfactory neuron adhesion to two laminin family members, and promotes intercellular adhesion. Both activities are dose-dependent, and are independent of integrin-mediated mechanisms. We have thus found that L-14 can serve two distinct adhesive functions in vitro, and propose that L-14 in vivo can promote olfactory axon fasciculation by crosslinking adjacent axons and promote axonal adhesion to the extracellular matrix.

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Mannose-binding Lectin-deficient Mice Are Susceptible to Infection with Staphylococcus aureus

Journal of Experimental Medicine ◽

10.1084/jem.20032207 ◽

2004 ◽

Vol 199 (10) ◽

pp. 1379-1390 ◽

Cited By ~ 207

Author(s):

Lei Shi ◽

Kazue Takahashi ◽

Joseph Dundee ◽

Sarit Shahroor-Karni ◽

Steffen Thiel ◽

...

Keyword(s):

Staphylococcus Aureus ◽

Susceptibility Gene ◽

Humoral Response ◽

Mannose Binding Lectin ◽

Host Responses ◽

Mannose Binding ◽

Disease Susceptibility Gene ◽

Binding Lectin

Gram-positive organisms like Staphylococcus aureus are a major cause of morbidity and mortality worldwide. Humoral response molecules together with phagocytes play a role in host responses to S. aureus. The mannose-binding lectin (MBL, also known as mannose-binding protein) is an oligomeric serum molecule that recognizes carbohydrates decorating a broad range of infectious agents including S. aureus. Circumstantial evidence in vitro and in vivo suggests that MBL plays a key role in first line host defense. We tested this contention directly in vivo by generating mice that were devoid of all MBL activity. We found that 100% of MBL-null mice died 48 h after exposure to an intravenous inoculation of S. aureus compared with 45% mortality in wild-type mice. Furthermore, we demonstrated that neutrophils and MBL are required to limit intraperitoneal infection with S. aureus. Our study provides direct evidence that MBL plays a key role in restricting the complications associated with S. aureus infection in mice and raises the idea that the MBL gene may act as a disease susceptibility gene against staphylococci infections in humans.

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Recognition ofCandida albicansby Mannan‐Binding Lectin In Vitro and In Vivo

The Journal of Infectious Diseases ◽

10.1086/503804 ◽

2006 ◽

Vol 193 (11) ◽

pp. 1589-1597 ◽

Cited By ~ 52

Author(s):

Joseph B. Lillegard ◽

Robert B. Sim ◽

Peter Thorkildson ◽

Marcellene A. Gates ◽

Thomas R. Kozel

Keyword(s):

Mannan Binding Lectin ◽

Binding Lectin

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Antimicrobial peptide LL-37 and recombinant human mannose-binding lectin express distinct age- and pathogen-specific antimicrobial activity in human newborn cord blood in vitro

F1000Research ◽

10.12688/f1000research.14736.1 ◽

2018 ◽

Vol 7 ◽

pp. 616 ◽

Cited By ~ 4

Author(s):

Annette Scheid ◽

Ning Li ◽

Carleen Jeffers ◽

Francesco Borriello ◽

Sweta Joshi ◽

...

Keyword(s):

Antimicrobial Activity ◽

Antifungal Activity ◽

Antimicrobial Peptide ◽

Cord Blood ◽

Mannose Binding Lectin ◽

Human Cord Blood ◽

Mannose Binding ◽

Binding Lectin

Background: There is a need to prevent and treat infection in newborns. One approach is administration of antimicrobial proteins and peptides (APPs) such as LL-37, a membrane-active cathelicidin antimicrobial peptide, and mannose-binding lectin (MBL), a pattern-recognition protein that binds to microbial surface polysaccharides resulting in opsonization and complement activation. Low plasma/serum levels of LL-37 and of MBL have been correlated with infection and exogenous administration of these agents may enhance host defense. Methods: The antimicrobial activity of LL-37 (15 µg/ml) or rMBL (0.5, 2 and 10 µg/ml) was tested in hirudin-anticoagulated preterm and term human cord blood (N = 12–14) against Staphylococcus aureus (SA) USA 300 (2x104 CFU/ml), Staphylococcus epidermis (SE) 1457 (2x104 CFU/ml) and Candida albicans (CA) SC5314 (1x104 CFU/ml). After incubation (1, 45, or 180 min), CFUs were enumerated by plating blood onto agar plates. Supernatants were collected for measurement of MBL via ELISA. Results: Preterm cord blood demonstrated impaired endogenous killing capacity against SA and SE compared to term blood. Addition of LL-37 strongly enhanced antimicrobial/antifungal activity vs SA, SE and CA in term blood and SE and CA in preterm blood. By contrast, rMBL showed modest fungistatic activity vs CA in a sub-analysis of term newborns with high basal MBL levels. Baseline MBL levels varied within preterm and term cohorts with no correlation to gestational age. In summary, exogenous LL-37 demonstrated significant antimicrobial activity against SA, SE and CA in term and SE and CA in preterm human blood tested in vitro. rMBL demonstrated modest antifungal activity in term cord blood of individuals with high baseline MBL levels. Conclusions: To the extent that our in vitro results predict the effects of APPs in vivo, development of APPs for prevention and treatment of infection should take into account host age as well as the target pathogen.

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