What with all of the concern recently on the dogs who have developed heart disease, I've gotten a lot of questions on whether we know the cause and what to do about it. There are a couple of great summaries that I will refer you to, but the short answer from me is this - the problems seem to be associated solely with small companies or homemade diets. From what I can tell, none of the larger, very well established companies are involved. So that's the answer for now - I would try to stick with large, well established companies and not just one of them. I've always said that it's safer to rotate between a few different companies and this is a good example of why I recommend that.
That's not what this is about though - there has recently been some kerfuffle claiming that the reason for this crisis is plant lectins. I was curious and did some research myself. This is what I've come up with.
Lectins in Pet foods
Susan G. Wynn, DVM, DACVN
Antinutritional factors appear, as a whole, to benefit plants by
deterring predators and microbes. The varying degrees of toxicity to animals,
insects and microbes have been exploited in studies that explore medical
applications.
Plant defenses include low molecular weight compounds (alkaloids,
terpenoids, tannins, and glycosides), and proteins (lectins,
ribosome-inactivating proteins (RIPs), protease inhibitors, a-amylase
inhibitors, ureases, arcelins, canatoxins, antimicrobial peptides and
pore-forming toxins). The proteins tend to accumulate in vulnerable (i.e.
edible) parts of the plants - seeds and storage tissues.
The first toxic carbohydrate-binding protein - a lectin called ricin - was discovered in
the seeds of castor beans in 1888. Lectins have been reported in bean, tomato,
potato, banana and garlic. Lectins are ubiquitous among plants and to date,
several hundred have been identified. In addition to plants, animals, insects,
viruses, fungi and bacteria also synthesize lectins.
Lectins are globular proteins of non-immune origin that have specific
CHO-binding activity and have at least one non-catalytic domain that binds
reversibly with specific mono- or oligosaccharides without altering the
substrate. Binding is specific but diverse, with some lectins recognizing
monosaccharides (such as mannose, glucose, galactose, and fucose). However most
plant lectins preferentially bind oligosaccharides like N- and O-linked glycans. Thus far, 12 lectin families have been described, based on sequence
similarities and evolutionary relationships.
Toxicity is, in part, determined by resistance to proteolysis by gut
enzymes. Lectin toxicity varies widely, from antinutritional activity to lethal
effects. Common beans (Phaseolus vulgaris) contain phytohemagglutinin (PHA)
which is highly toxic. In the gastrointestinal tract, lectins can act as toxic
allergens and hemagglutinins. If lectins bind epithelial cells in the animal
digestive tract, the activity at these receptors may have adverse effects on
the cellular morphology and metabolism of the stomach and/or the small
intestine, and can alter permeability and activate signaling cascades that
alter intermediary metabolism (Vasconcelos, 2004).
Most of our knowledge about the anti-nutritional effects of lectin is
derived from animal experiments, using purified lectins, with very few clinical
studies in humans. Short term experiments in rats have shown that purified
lectins from beans or soybeans damaged the epithelial cells. led to
enlargement of the small intestine, stimulated hypertrophy and hyperplasia of
the pancreas, and impaired the growth of rats in the studies. In addition to
disrupting the cell membrane, lectins can inhibit the activity of brush border
enzymes. If the activity of lectins is marked enough and not modulated by the
intraluminal food matrix, the potential toxicity is primarily interference with
protein and carbohydrate digestion and absorption. It does appear that lectins
must bind to the gut epithelium to cause damage, and any that pass through the
gut are harmless.
Phytohemagglutinins (PHA) from Phaseolus vulgaris, the common bean
including black turtle bean, string bean, flageolet bean, kidney bean, pea
bean, pink bean, pinto bean, white bean, yellow bean, cranberry and borlotti
bean, and so on, have been studied extensively. PHA is a mitogen and has been
used in laboratory studies to stimulate cellular activity. PHA binds strongly
to the brush border of the small intestine, and disrupts normal development of
intestinal microvilli (in rats). Since lectins remain attached to the
epithelial surface, they may also inhibit plasma membrane repair resulting in a
net loss of cells.
Even endogenous lectins have been implicated in GI damage - several
galectins appear to be involved in the development and progression of
inflammatory bowel disease and intestinal tumors. Galectins are a group of
mammalian lectins which are involved in cell-to-cell adhesion, growth
regulation, signalling and cytokine secretion.
A potential secondary toxic effect of undigested lectin in the small
intestine is to lead to overgrowth of coliform bacteria, possibly due to the
intraluminal changes in nutrient content induced by increased mucus secretion,
epithelial cell loss, serum protein leakage and reduced digestion of dietary
protein.
As additional adverse effect is stimulation of an allergic response. When systemically absorbed intact, PHA can lead to a Th2 response and a
Type I (IgE-mediated) allergy, at least in rat studies.
What isn’t understood is the physiologic and nutritional significance of
low level, chronic ingestion of lectins and other anti-nutritional factors when
taken in as part of the natural diet, cooked or raw, or even whether beans can
be considered a natural part of the canine or feline diet. Soy products, for
instance, retain 5-20% of the trypsin inhibitory activity originally present in
raw soybeans. While some have theorized that the amounts of trypsin and
chymotrypsin produced by a human could be completely inhibited by ingestion of
raw soybeans or 200 g of other raw legume containing 2 grams of inhibitors,
humans do not routinely eat raw beans.
Lectins have been subjected to industrial and experimental processing
methods such as steam heating, autoclaving, extrusion and dry roasting in order
to study their antinutritional effects. Although lectins are in general considered heat-resistant, it has been
well established that they can be inactivated after cooking (around 100C or
212 farenheit) for short periods of time (up to about 15 minutes), with an
improvement of the accessibility of the protein to enzymatic attack(Coffey et
al., 1992) (He 2018 p78). He (2018) reports that the navy bean (Phaseolus
vulgaris) hemagglutinin (HA) lectin “could be fully eliminated at 121C for 5
minutes after the autoclaving treatment, and white bean (Phaseolus vulgaris)
lectin could be fully inactivated after steam treatment of 100C for 15 minutes;
extrusion treatment of 145C for 16 minutes resulted in 98% reduction in the HA
of small red bean (Phaseolus vulgaris) lectin, as well as 99% reduction in the
HA of navy bean (Phaseolus vulgaris) lectin observed with the dry roasting
treatment at 200C for minutes (Van der Poel, 1990; Shimelis and Rakshit,
2007)." Purified PHA was subjected to high pressure pasteurization (HPP)
and while low pressure (150 mPA) did not change the hemagglutinin activity,
high pressure (450 mPA) led to a ‘noticeable decrease in the hemagglutinin
activity”. To summarize, normal cooking temperatures for 15 minutes appear to inactivate most of the undesirable activity, as does high pressure pasteurization.
Lectins may have biomedical applications and are being investigated for
potential anti-tumor activity. The antiviral, antifungal and insecticidal
properties of some toxic plant proteins has given them potential use in agriculture.
Lectins have been used to target malignant cells for specific drug delivery,
especially Concanavalin A and BSA. Some PHAs may bind human tumor cells and
elicit production of inducible NO synthasae which is anticarcinogenic. PHA has also been shown to inhibit HIV replication. PHAs have also been shown to enhance the immune response against infections in general as it stimulates lymphocyte replication.
Extracts of beans are marketed for weight loss with the premise that PHA inhibit carbohydrate absorption and metabolism. These effects are seen using isolated, uncooked plant lectin - obviously a plate of cooked beans would not have the same benefit!
Summary
While lectins do have adverse effects on the Gi tract of rats when
administered as an isolated treatment, similar damage has not been demonstrated
when lectin-containing foods are ingested as a normal part of the diet in
humans. Reviewers have concluded that when properly cooked, lectin-containing
foods are unlikely to pose any risk to humans. While beans in significant
amounts are not a natural component of the feline diet, they may or may not be
a natural part of the canine diet. In pet foods, lectin-containing foods are
extruded or canned, which should destroy most of the antinutritional activity.
In addition, these foods are only one component in a recipe containing other
ingredients, which are usually meats. Vegan diets containing no animal protein
may have enough residual lectin activity to be of concern, especially if they
have been subjected to dry heat only, as wet heat is more effective. The recent crisis in dogs who develop
dilated cardiomyopathy is unlikely to be related to the lectin content of bean-
or lentil- containing foods because many kinds of foods have been implicated,
including some that contain no beans or other foods high in lectins. Further,
if lectins were causing mucosal damage, why would the metabolism or absorption
of taurine in particular be targeted? Damage from lectins appears to have a
much broader effect, resulting in a leaky gut that should theoretically have
much more systemic results. But probably only if you are a rat, eating pure lectin.